5v1x
From Proteopedia
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==Carbon Sulfoxide lyase, Egt2 Y134F in complex with its substrate== | ==Carbon Sulfoxide lyase, Egt2 Y134F in complex with its substrate== | ||
| - | <StructureSection load='5v1x' size='340' side='right' caption='[[5v1x]], [[Resolution|resolution]] 2.56Å' scene=''> | + | <StructureSection load='5v1x' size='340' side='right'caption='[[5v1x]], [[Resolution|resolution]] 2.56Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5v1x]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v1x]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Neucr Neucr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1X FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8VV:(2~{S})-3-[2-[(2~{R})-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfinyl-1~{H}-imidazol-4-yl]-2-(trimethyl-$l^{4}-azanyl)propanoic+acid'>8VV</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8VV:(2~{S})-3-[2-[(2~{R})-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfinyl-1~{H}-imidazol-4-yl]-2-(trimethyl-$l^{4}-azanyl)propanoic+acid'>8VV</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">egt-2, NCU11365 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367110 NEUCR])</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=5v1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1x OCA], [http://pdbe.org/5v1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1x RCSB], [http://www.ebi.ac.uk/pdbsum/5v1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1x ProSAT]</span></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=5v1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1x OCA], [http://pdbe.org/5v1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1x RCSB], [http://www.ebi.ac.uk/pdbsum/5v1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent pyridoxal 5'-phosphate (PLP)-mediated C-S lyase reaction leads to the net transfer of a sulfur atom from a cysteine to a histidine. In this study, we structurally and mechanistically characterized a PLP-dependent C-S lyase Egt2, which mediates the sulfoxide C-S bond cleavage in ergothioneine biosynthesis. A cation-pi interaction between substrate and enzyme accounts for Egt2's preference of sulfoxide over thioether as a substrate. Using mutagenesis and structural biology, we captured three distinct states of the Egt2 C-S lyase reaction cycle, including a labile sulfenic intermediate captured in Egt2 crystals. Chemical trapping and high-resolution mass spectrometry were used to confirm the involvement of the sulfenic acid intermediate in Egt2 catalysis. | ||
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| + | Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.,Irani S, Naowarojna N, Tang Y, Kathuria KR, Wang S, Dhembi A, Lee N, Yan W, Lyu H, Costello CE, Liu P, Zhang YJ Cell Chem Biol. 2018 May 17;25(5):519-529.e4. doi:, 10.1016/j.chembiol.2018.02.002. Epub 2018 Mar 1. PMID:29503207<ref>PMID:29503207</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5v1x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neucr]] | ||
[[Category: Irani, S]] | [[Category: Irani, S]] | ||
[[Category: Zhang, Y]] | [[Category: Zhang, Y]] | ||
Revision as of 08:15, 20 March 2019
Carbon Sulfoxide lyase, Egt2 Y134F in complex with its substrate
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Categories: Large Structures | Neucr | Irani, S | Zhang, Y | C-s lyase | Lyase | Plp dependent
