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3ri6

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==A Novel Mechanism of Sulfur Transfer Catalyzed by O-Acetylhomoserine Sulfhydrylase in Methionine Biosynthetic Pathway of Wolinella succinogenes==
==A Novel Mechanism of Sulfur Transfer Catalyzed by O-Acetylhomoserine Sulfhydrylase in Methionine Biosynthetic Pathway of Wolinella succinogenes==
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<StructureSection load='3ri6' size='340' side='right' caption='[[3ri6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='3ri6' size='340' side='right'caption='[[3ri6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ri6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29543 Atcc 29543]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RI6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ri6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RI6 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mety, WS1012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=844 ATCC 29543])</td></tr>
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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]] 2.2&#8491;</td></tr>
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<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=3ri6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ri6 OCA], [http://pdbe.org/3ri6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ri6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ri6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ri6 ProSAT]</span></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=3ri6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ri6 OCA], [https://pdbe.org/3ri6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ri6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ri6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ri6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7M9C8_WOLSU Q7M9C8_WOLSU]
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O-Acetylhomoserine sulfhydrylase (OAHS) is a pyridoxal 5'-phosphate (PLP) dependent sulfide-utilizing enzyme in the L-cysteine and L-methionine biosynthetic pathways of various enteric bacteria and fungi. OAHS catalyzes the conversion of O-acetylhomoserine to homocysteine using sulfide in a process known as direct sulfhydrylation. However, the source of the sulfur has not been identified and no structures of OAHS have been reported in the literature. Here, the crystal structure of Wolinella succinogenes OAHS (MetY) determined at 2.2 A resolution is reported. MetY crystallized in space group C2 with two monomers in the asymmetric unit. Size-exclusion chromatography, dynamic light scattering and crystal packing indicate that the biological unit is a tetramer in solution. This is further supported by the crystal structure, in which a tetramer is formed using a combination of noncrystallographic and crystallographic twofold axes. A search for structurally homologous proteins revealed that MetY has the same fold as cystathionine gamma-lyase and methionine gamma-lyase. The active sites of these enzymes, which are also PLP-dependent, share a high degree of structural similarity, suggesting that MetY belongs to the gamma-elimination subclass of the Cys/Met metabolism PLP-dependent family of enzymes. The structure of MetY, together with biochemical data, provides insight into the mechanism of sulfur transfer to a small molecule via a protein thiocarboxylate intermediate.
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A novel mechanism of sulfur transfer catalyzed by O-acetylhomoserine sulfhydrylase in the methionine-biosynthetic pathway of Wolinella succinogenes.,Tran TH, Krishnamoorthy K, Begley TP, Ealick SE Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):831-8. Epub 2011, Sep 8. PMID:21931214<ref>PMID:21931214</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ri6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 29543]]
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[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Wolinella succinogenes]]
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[[Category: Ealick, S E]]
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[[Category: Begley TP]]
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[[Category: Krishnamoorthy, K]]
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[[Category: Ealick SE]]
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[[Category: Tran, T H]]
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[[Category: Krishnamoorthy K]]
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[[Category: Cys/met metabolism]]
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[[Category: Tran TH]]
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[[Category: Direct sulfhydrylation]]
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[[Category: Gamma-elimination]]
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[[Category: O-acetylhomoserine]]
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[[Category: Protein thiocarboxylate]]
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[[Category: Pyridoxal-5'-phosphate]]
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[[Category: Transferase]]
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[[Category: Wolinella succinogenes o-acetylhomoserine sulfhydrylase]]
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Current revision

A Novel Mechanism of Sulfur Transfer Catalyzed by O-Acetylhomoserine Sulfhydrylase in Methionine Biosynthetic Pathway of Wolinella succinogenes

PDB ID 3ri6

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