https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Taylor+Telford 2026-09-23T11:17:09Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3122826 2019-12-09T01:31:25Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> <br /> This is a &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein. Overall, there doesn't seem to be any dominant hydrophobic or hydrophillic regions of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity &lt;ref&gt;PMID 31292192&lt;/ref&gt;. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> LSDs are in the functional protein family called carotenoid cleavage oxygenases (CCOs). They are characterized by their cleavage of the double bond found in carotenoids. The binding site has ferrous iron supported by histidines and is kept in close proximity to the scissile double bond. There are two suggested mechanisms for LSD cleavage. McAndrew ''et al.'' suggested the hydroxystilbenoid is activated by enzyme-catalyzed deprotonation of the 4-hydroxy group. This causes electron delocalization toward the ferrous iron (-superoxo electrophile). The second proposed mechanism suggested by Sui ''et al.'' says that the pi bond electron density from the scissile double bond is redistributed to the iron-oxy complex to form an iron peroxo-substrate cation intermediate. In either case, deprotonation of the hydoxyl group is critical and assisted by the catalytic triad.&lt;ref&gt;PMID 31292192&lt;/ref&gt;<br /> <br /> The enzyme serves to lower the activation energy and assist in the cleavage and transformation of the lignostilbene to two vanillins.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3122819 2019-12-09T01:23:29Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> <br /> This is a &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein. Overall, there doesn't seem to be any dominant hydrophobic or hydrophillic regions of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity &lt;ref&gt;PMID 31292192&lt;/ref&gt;. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> LSDs are in the functional protein family called carotenoid cleavage oxygenases (CCOs). They are characterized by their cleavage of the double bond found in carotenoids. The binding site has ferrous iron supported by histidines and is kept in close proximity to the scissile double bond. There are two suggested mechanisms for LSD cleavage. McAndrew ''et al.'' suggested the hydroxystilbenoid is activated by enzyme-catalyzed deprotonation of the 4-hydroxy group. This causes electron delocalization toward the ferrous iron (-superoxo electrophile). The second proposed mechanism suggested by Sui ''et al.'' says that the pi bond electron density from the scissile double bond is redistributed to the iron-oxy complex to form an iron peroxo-substrate cation intermediate. In either case, deprotonation of the hydoxyl group is critical and assisted by the catalytic triad.&lt;ref&gt;PMID 31292192&lt;/ref&gt;<br /> <br /> <br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3122785 2019-12-08T23:45:47Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> <br /> This is a &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein. Overall, there doesn't seem to be any dominant hydrophobic or hydrophillic regions of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity &lt;ref&gt;PMID 31292192&lt;/ref&gt;. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118574 2019-11-30T23:56:41Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity &lt;ref&gt;PMID 31292192&lt;/ref&gt;. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118572 2019-11-30T23:54:54Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118543 2019-11-30T21:03:38Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt; are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118541 2019-11-30T20:54:36Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> <br /> Important &lt;scene name='82/823092/Active_site_interactions/1'&gt;interactions in the active site&lt;/scene&gt;.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118414 2019-11-30T00:58:22Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> &lt;scene name='82/823092/Hydrophobic_spacefill/1'&gt;Hydrophobicity-focused&lt;/scene&gt; view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=File:Ligand_hydrophobicity.png&diff=3118411 2019-11-30T00:54:26Z

<p>Taylor Telford: </p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118409 2019-11-30T00:54:12Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity.png]]<br /> <br /> Hydrophobicity-focused view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=File:Spacefill_hydrophobicity.png&diff=3118408 2019-11-30T00:53:31Z

<p>Taylor Telford: uploaded a new version of &quot;Image:Spacefill hydrophobicity.png&quot;</p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=File:Spacefill_hydrophobicity.png&diff=3118407 2019-11-30T00:51:40Z

<p>Taylor Telford: uploaded a new version of &quot;Image:Spacefill hydrophobicity.png&quot;</p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=File:Spacefill_hydrophobicity.png&diff=3118405 2019-11-30T00:47:54Z

<p>Taylor Telford: </p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118404 2019-11-30T00:47:20Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> When you look at the &lt;scene name='82/823092/Spacefill_lsda/1'&gt;spacefill view&lt;/scene&gt; of the protein dimer you see that the binding pocket accessibility is very restrictive.<br /> [[Image:spacefill hydrophobicity.png]][[Image:ligand hydrophobicity]]<br /> <br /> Hydrophobicity-focused view of the protein.<br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118398 2019-11-30T00:18:43Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> <br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/2'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118397 2019-11-30T00:16:58Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a &lt;scene name='82/823092/Seven-bladed_beta_propeller/1'&gt;seven-bladed ß-propeller&lt;/scene&gt;, typical of the carotenoid cleavage oxygenases.<br /> <br /> <br /> <br /> The &lt;scene name='82/823092/Catalytic_triad/1'&gt;catalytic triad&lt;/scene&gt; of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118394 2019-11-29T23:51:28Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> LsdA appears when crystallized as two LsdA protomers in one asymmetric unit as a dimer. The &lt;scene name='82/823092/Secondary_and_tertiary_struct/1'&gt;secondary and tertiary structure&lt;/scene&gt; of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a seven-bladed ß-propeller, typical of the carotenoid cleavage oxygenases. <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118389 2019-11-29T23:23:27Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules.<br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118388 2019-11-29T22:42:50Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> ==== '''Lignostilbene''' ====<br /> [[Image:lignostilbene.png]]<br /> ==== '''Vanillin''' ====<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118387 2019-11-29T22:42:29Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> === '''Lignostilbene''' ===<br /> [[Image:lignostilbene.png]]<br /> === '''Vanillin''' ===<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118384 2019-11-29T22:21:34Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> == '''Lignostilbene-α,ß-dioxygenase A structural features and important functional residues''' ==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == '''Functions and Biological Relevance''' ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> == '''Lignostilbene''' ==<br /> [[Image:lignostilbene.png]]<br /> == '''Vanillin''' ==<br /> [[Image:Vanillin.png]]<br /> == '''Broader Implications''' ==<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == '''References''' ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118383 2019-11-29T22:19:54Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> <br /> == Lignostilbene ==<br /> [[Image:lignostilbene.png]]<br /> == Vanillin ==<br /> [[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118379 2019-11-29T22:14:40Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='420' side='right' caption='LsdA phenylazophenol complex' scene=''&gt;<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118378 2019-11-29T22:10:41Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;PMID 31292192&lt;/ref&gt;.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118377 2019-11-29T22:10:09Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;31292192&lt;/ref&gt;.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118376 2019-11-29T22:08:48Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;RA119.009428&lt;/ref&gt;.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118375 2019-11-29T22:08:07Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;jbc.RA119.009428&lt;/ref&gt;.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118374 2019-11-29T22:05:41Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A structural features and important functional residues==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118373 2019-11-29T22:02:37Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6ojt' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane.<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118372 2019-11-29T22:01:07Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='420' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118371 2019-11-29T21:59:15Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='420' side='right' caption='Caption for this structure' scene=''&gt;<br /> <br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage via oxygenolytic fission of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass from industry that scientists are interested in finding ways to break down to simpler and useful materials such as biofuels and commodity chemicals. Though natural occurring lignostilbenoids are rare, they are a very comm on byproduct of industry due to condensation reactions. Other lignin-based stilbenes are thought to be produces from bacterial catabolic processing of diaryl propane and phenylcoumarane &lt;ref&gt;<br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118359 2019-11-29T21:22:47Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='420' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials. <br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118358 2019-11-29T21:22:17Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='380' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials. <br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118311 2019-11-29T16:46:11Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials. <br /> <br /> '''Lignostilbene'''[[Image:lignostilbene.png]]'''Vanillin'''[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118310 2019-11-29T16:44:15Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials. <br /> <br /> Lignostilbene[[Image:lignostilbene.png]]Vanillin[[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118308 2019-11-29T16:42:38Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials.<br /> <br /> [[Image:lignostilbene.png]][[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118306 2019-11-29T16:40:07Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Lignostilbene-α,ß-dioxygenase A (LsdA) structure and function==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). <br /> <br /> [[Image:lignostilbene.png]][[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118301 2019-11-29T16:31:49Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. <br /> <br /> [[Image:lignostilbene.png]][[Image:Vanillin.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=File:Vanillin.png&diff=3118300 2019-11-29T16:30:43Z

<p>Taylor Telford: </p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118299 2019-11-29T16:29:55Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. <br /> <br /> [[Image:lignostilbene.png]][[Image:Vanillin]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118295 2019-11-29T16:26:40Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. <br /> <br /> [[Image:lignostilbene.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=File:Lignostilbene.png&diff=3118290 2019-11-29T16:23:51Z

<p>Taylor Telford: </p> <hr /> <div></div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118288 2019-11-29T16:23:31Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules.<br /> <br /> [https://www.brenda-enzymes.org/structure.php?n=90374][[Image:lignostilbene.png]]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118287 2019-11-29T16:19:39Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules.<br /> <br /> [https://www.brenda-enzymes.org/structure.php?n=90374]<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118281 2019-11-29T16:07:01Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules.<br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford https://proteopedia.org/index.php?title=Sandbox_Reserved_1568&diff=3118279 2019-11-29T15:57:20Z

<p>Taylor Telford: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}&lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='6OJT' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function(s) and Biological Relevance ==<br /> <br /> == Broader Implications ==<br /> <br /> == Structural highlights and structure-function relationships ==<br /> <br /> == Energy Transformation ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Taylor Telford