5z0q: Difference between revisions

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-'''Unreleased structure'''
-The entry 5z0q is ON HOLD  until Paper Publication
+==Crystal Structure of OvoB==
+<StructureSection load='5z0q' size='340' side='right' caption='[[5z0q]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5z0q]] is a 12 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z0Q FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z0q OCA], [http://pdbe.org/5z0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z0q RCSB], [http://www.ebi.ac.uk/pdbsum/5z0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z0q ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5z0q" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cai, Y J]]
+[[Category: Huang, P]]
+[[Category: Liu, P H]]
+[[Category: Wu, L]]
+[[Category: Zhou, J H]]
+[[Category: Aminotransferase]]
+[[Category: Biosynthesis]]
+[[Category: Biosynthetic protein]]
+[[Category: C-s lyase]]
+[[Category: Ovothiol some]]
+[[Category: Plp coenzyme]]
+[[Category: Transferase]]