Sandbox Reserved 1068: Difference between revisions

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[[Image:Capture.PNG|300 px|left|thumb|'''Figure 2''': Monomeric ribbon diagram of MbtI with active site cleft highlighted with a white circle. Generated from [[3log]] (3a)]]

The crystal asymmetric unit was found to contain <scene name='69/694235/3log/11'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme <ref name= "3a">PMID 16923875</ref>. There are no significant structural changes between the four monomers excepts from the localized differences in the active site <ref name= "3a"/>. The overall molecular structure consist of a polypeptide of 450 residues that forms <scene name='69/694235/Alpha_helics/2'>one large single domain</scene> with a similar fold to other chromate-utilizing enzymes <ref name="3a"/>. The core of the protein is formed by <scene name='69/694234/Beta_sheets/1'>21 ~~Beta~~ sheets </scene>folded into a twisted beta-sandwich. The protein's core is then surrounded by <scene name='69/694235/Beta_sheets/4'>10 alpha helices</scene><ref name="3a"/>. The active site was identified by comparison to the product bound forms of Irp9 and TrpE and is situated in a cleft that is about 12Å in length, 10Å deep, and 7Å wide <ref name="3a"/>. One side of the groove is formed by β21, C-terminal helix, and α11 while the other side of the groove is formed by β16-17 loop, helix α7, and β15-α6 loop (~~figure~~ 2)<ref name="3a"/>. The β19-20 and β12-13 loops make up the bottom of the active side cleft (Figure 2) <ref name="3a">PMID:16923875</ref>.

The crystal asymmetric unit was found to contain <scene name='69/694235/3log/11'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme <ref name= "3a">PMID 16923875</ref>. There are no significant structural changes between the four monomers excepts from the localized differences in the active site <ref name= "3a"/>. The overall molecular structure consist of a polypeptide of 450 residues that forms <scene name='69/694235/Alpha_helics/2'>one large single domain</scene> with a similar fold to other chromate-utilizing enzymes <ref name="3a"/>. The core of the protein is formed by <scene name='69/694234/Beta_sheets/1'>21 beta sheets </scene>folded into a twisted beta-sandwich. The protein's core is then surrounded by <scene name='69/694235/Beta_sheets/4'>10 alpha helices</scene><ref name="3a"/>. The active site was identified by comparison to the product bound forms of [[Irp9]] and [[TrpE]] and is situated in a cleft that is about 12Å in length, 10Å deep, and 7Å wide <ref name="3a"/>. One side of the groove is formed by β21, C-terminal helix, and α11 while the other side of the groove is formed by β16-17 loop, helix α7, and β15-α6 loop (Figure 2)<ref name="3a"/>. The β19-20 and β12-13 loops make up the bottom of the active side cleft (Figure 2) <ref name="3a">PMID:16923875</ref>.

Sandbox Reserved 1068: Difference between revisions

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Revision as of 23:11, 26 April 2015 view source Stephanie Raynor (talk \| contribs) 145 edits No edit summary ← Older edit		Revision as of 23:14, 26 April 2015 view source Stephanie Raynor (talk \| contribs) 145 edits No edit summary Newer edit →
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	[[Image:Capture.PNG\|300 px\|left\|thumb\|'''Figure 2''': Monomeric ribbon diagram of MbtI with active site cleft highlighted with a white circle. Generated from [[3log]] (3a)]]		[[Image:Capture.PNG\|300 px\|left\|thumb\|'''Figure 2''': Monomeric ribbon diagram of MbtI with active site cleft highlighted with a white circle. Generated from [[3log]] (3a)]]

	The crystal asymmetric unit was found to contain <scene name='69/694235/3log/11'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme <ref name= "3a">PMID 16923875</ref>. There are no significant structural changes between the four monomers excepts from the localized differences in the active site <ref name= "3a"/>. The overall molecular structure consist of a polypeptide of 450 residues that forms <scene name='69/694235/Alpha_helics/2'>one large single domain</scene> with a similar fold to other chromate-utilizing enzymes <ref name="3a"/>. The core of the protein is formed by <scene name='69/694234/Beta_sheets/1'>21 ~~Beta~~ sheets </scene>folded into a twisted beta-sandwich. The protein's core is then surrounded by <scene name='69/694235/Beta_sheets/4'>10 alpha helices</scene><ref name="3a"/>. The active site was identified by comparison to the product bound forms of Irp9 and TrpE and is situated in a cleft that is about 12Å in length, 10Å deep, and 7Å wide <ref name="3a"/>. One side of the groove is formed by β21, C-terminal helix, and α11 while the other side of the groove is formed by β16-17 loop, helix α7, and β15-α6 loop (~~figure~~ 2)<ref name="3a"/>. The β19-20 and β12-13 loops make up the bottom of the active side cleft (Figure 2) <ref name="3a">PMID:16923875</ref>.		The crystal asymmetric unit was found to contain <scene name='69/694235/3log/11'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme <ref name= "3a">PMID 16923875</ref>. There are no significant structural changes between the four monomers excepts from the localized differences in the active site <ref name= "3a"/>. The overall molecular structure consist of a polypeptide of 450 residues that forms <scene name='69/694235/Alpha_helics/2'>one large single domain</scene> with a similar fold to other chromate-utilizing enzymes <ref name="3a"/>. The core of the protein is formed by <scene name='69/694234/Beta_sheets/1'>21 beta sheets </scene>folded into a twisted beta-sandwich. The protein's core is then surrounded by <scene name='69/694235/Beta_sheets/4'>10 alpha helices</scene><ref name="3a"/>. The active site was identified by comparison to the product bound forms of [[Irp9]] and [[TrpE]] and is situated in a cleft that is about 12Å in length, 10Å deep, and 7Å wide <ref name="3a"/>. One side of the groove is formed by β21, C-terminal helix, and α11 while the other side of the groove is formed by β16-17 loop, helix α7, and β15-α6 loop (Figure 2)<ref name="3a"/>. The β19-20 and β12-13 loops make up the bottom of the active side cleft (Figure 2) <ref name="3a">PMID:16923875</ref>.