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5z0q

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(New page: '''Unreleased structure''' The entry 5z0q is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (08:43, 22 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5z0q is ON HOLD
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==Crystal Structure of OvoB==
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<StructureSection load='5z0q' size='340' side='right'caption='[[5z0q]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z0q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_tasmaniensis_Et1/99 Erwinia tasmaniensis Et1/99]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z0Q FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5z0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z0q OCA], [https://pdbe.org/5z0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z0q RCSB], [https://www.ebi.ac.uk/pdbsum/5z0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z0q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2VJB8_ERWT9 B2VJB8_ERWT9]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ovothiols are thiolhistidine derivatives. The first step of ovothiol biosynthesis is OvoA-catalyzed oxidative coupling between histidine and cysteine. In this report, the remaining steps of ovothiol A biosynthesis were reconstituted in vitro. ETA_14770 (OvoB) was reported as a PLP-dependent sulfoxide lyase, responsible for mercaptohistidine production. OvoA was found to be a bifunctional enzyme, which mediates both oxidative C-S bond formation and methylation of mercaptohistidine to afford ovothiol A. Besides reconstituting the whole biosynthetic pathway, two unique features proposed in the literature were also examined: a potential cysteine-recycling mechanism of the C-S lyase (OvoB) and the selectivity of the pi- N methyltransferase.
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Authors:
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In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions.,Naowarojna N, Huang P, Cai Y, Song H, Wu L, Cheng R, Li Y, Wang S, Lyu H, Zhang L, Zhou J, Liu P Org Lett. 2018 Sep 7;20(17):5427-5430. doi: 10.1021/acs.orglett.8b02332. Epub, 2018 Aug 24. PMID:30141637<ref>PMID:30141637</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5z0q" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Erwinia tasmaniensis Et1/99]]
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[[Category: Large Structures]]
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[[Category: Cai YJ]]
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[[Category: Huang P]]
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[[Category: Liu PH]]
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[[Category: Wu L]]
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[[Category: Zhou JH]]

Current revision

Crystal Structure of OvoB

PDB ID 5z0q

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