5z0q
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of OvoB== | |
| + | <StructureSection load='5z0q' size='340' side='right'caption='[[5z0q]], [[Resolution|resolution]] 2.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2VJB8_ERWT9 B2VJB8_ERWT9] | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5z0q" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Erwinia tasmaniensis Et1/99]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cai YJ]] | ||
| + | [[Category: Huang P]] | ||
| + | [[Category: Liu PH]] | ||
| + | [[Category: Wu L]] | ||
| + | [[Category: Zhou JH]] | ||
Current revision
Crystal Structure of OvoB
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