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6fea
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(Difference between revisions)
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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=6fea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fea OCA], [http://pdbe.org/6fea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fea RCSB], [http://www.ebi.ac.uk/pdbsum/6fea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fea 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=6fea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fea OCA], [http://pdbe.org/6fea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fea RCSB], [http://www.ebi.ac.uk/pdbsum/6fea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fea ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Reduction of N2 by nitrogenases occurs at an organometallic iron cofactor that commonly also contains either molybdenum or vanadium. The well-characterized resting state of the cofactor does not bind substrate, so its mode of action remains enigmatic. Carbon monoxide was recently found to replace a bridging sulfide, but the mechanistic relevance was unclear. Here we report the structural analysis of vanadium nitrogenase with a bound intermediate, interpreted as a mu(2)-bridging, protonated nitrogen that implies the site and mode of substrate binding to the cofactor. Binding results in a flip of amino acid glutamine 176, which hydrogen-bonds the ligand and creates a holding position for the displaced sulfide. The intermediate likely represents state E6 or E7 of the Thorneley-Lowe model and provides clues to the remainder of the catalytic cycle. | ||
| + | |||
| + | A bound reaction intermediate sheds light on the mechanism of nitrogenase.,Sippel D, Rohde M, Netzer J, Trncik C, Gies J, Grunau K, Djurdjevic I, Decamps L, Andrade SLA, Einsle O Science. 2018 Mar 30;359(6383):1484-1489. doi: 10.1126/science.aar2765. PMID:29599235<ref>PMID:29599235</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6fea" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
A. vinelandii vanadium nitrogenase, turnover state
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