8s1j: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 8s1j~~ is ~~ON HOLD~~

==Crystal structure of t-anethole oxygenase from Stenotrophomonas maltophilia==

== Structural highlights ==

<table><tr><td colspan='2'>[[8s1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8S1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8S1J FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83Å</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8s1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8s1j OCA], [https://pdbe.org/8s1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8s1j RCSB], [https://www.ebi.ac.uk/pdbsum/8s1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8s1j ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Previously, some bacteria were shown to harbour enzymes capable of catalysing the oxidative cleavage of the double bond of t-anethole and related compounds. The cofactor dependence of these enzymes remained enigmatic due to a lack of biochemical information. We report on catalytic and structural details of a representative of this group of oxidative enzymes: t-anethole oxygenase from Stenotrophomonas maltophilia (TAO(Sm)). The bacterial enzyme could be recombinantly expressed and purified, enabling a detailed biochemical study that has settled the dispute on its cofactor dependence. We have established that TAO(Sm) contains a tightly bound b-type heme and merely depends on dioxygen for catalysis. It was found to accept t-anethole, isoeugenol and O-methyl isoeugenol as substrates, all being converted into the corresponding aromatic aldehydes without the need of any cofactor regeneration. The elucidated crystal structure of TAO(Sm) has revealed that it contains a unique active site architecture that is conserved for this distinct class of heme-containing bacterial oxygenases. Similar to other hemoproteins, TAO(Sm) has a histidine (His121) as proximal ligand. Yet, unique for TAOs, an arginine (Arg89) is located at the distal axial position. Site directed mutagenesis confirmed crucial roles for these heme-liganding residues and other residues that form the substrate binding pocket. In conclusion, the results reported here reveal a new class of bacterial heme-containing oxygenases that can be used for the cleavage of alkene double bonds, analogous to ozonolysis in organic chemistry.

~~Authors:~~ Rozeboom, H.J.~~, Fraaije, M~~.W.

Discovery of a new class of bacterial heme-containing CC cleaving oxygenases.,Purwani NN, Rozeboom HJ, Willers VP, Wijma HJ, Fraaije MW N Biotechnol. 2024 Jul 23;83:82-90. doi: 10.1016/j.nbt.2024.07.002. PMID:39053683<ref>PMID:39053683</ref>

~~Description: Crystal structure~~ of t-~~anethole oxygenase from Stenotrophomonas maltophilia~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Fraaije~~, M.W~~]]

[[Category: Rozeboom~~, H.J~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Stenotrophomonas maltophilia]]

[[Category: Fraaije MW]]

[[Category: Rozeboom HJ]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8s1j is ON HOLD
+==Crystal structure of t-anethole oxygenase from Stenotrophomonas maltophilia==
+<StructureSection load='8s1j' size='340' side='right'caption='[[8s1j]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8s1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8S1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8S1J FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8s1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8s1j OCA], [https://pdbe.org/8s1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8s1j RCSB], [https://www.ebi.ac.uk/pdbsum/8s1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8s1j ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Previously, some bacteria were shown to harbour enzymes capable of catalysing the oxidative cleavage of the double bond of t-anethole and related compounds. The cofactor dependence of these enzymes remained enigmatic due to a lack of biochemical information. We report on catalytic and structural details of a representative of this group of oxidative enzymes: t-anethole oxygenase from Stenotrophomonas maltophilia (TAO(Sm)). The bacterial enzyme could be recombinantly expressed and purified, enabling a detailed biochemical study that has settled the dispute on its cofactor dependence. We have established that TAO(Sm) contains a tightly bound b-type heme and merely depends on dioxygen for catalysis. It was found to accept t-anethole, isoeugenol and O-methyl isoeugenol as substrates, all being converted into the corresponding aromatic aldehydes without the need of any cofactor regeneration. The elucidated crystal structure of TAO(Sm) has revealed that it contains a unique active site architecture that is conserved for this distinct class of heme-containing bacterial oxygenases. Similar to other hemoproteins, TAO(Sm) has a histidine (His121) as proximal ligand. Yet, unique for TAOs, an arginine (Arg89) is located at the distal axial position. Site directed mutagenesis confirmed crucial roles for these heme-liganding residues and other residues that form the substrate binding pocket. In conclusion, the results reported here reveal a new class of bacterial heme-containing oxygenases that can be used for the cleavage of alkene double bonds, analogous to ozonolysis in organic chemistry.
-Authors: Rozeboom, H.J., Fraaije, M.W.
+Discovery of a new class of bacterial heme-containing CC cleaving oxygenases.,Purwani NN, Rozeboom HJ, Willers VP, Wijma HJ, Fraaije MW N Biotechnol. 2024 Jul 23;83:82-90. doi: 10.1016/j.nbt.2024.07.002. PMID:39053683<ref>PMID:39053683</ref>
-Description: Crystal structure of t-anethole oxygenase from Stenotrophomonas maltophilia
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Fraaije, M.W]]
+<div class="pdbe-citations 8s1j" style="background-color:#fffaf0;"></div>
-[[Category: Rozeboom, H.J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Stenotrophomonas maltophilia]]
+[[Category: Fraaije MW]]
+[[Category: Rozeboom HJ]]