5kh0
From Proteopedia
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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=5kh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh0 OCA], [http://pdbe.org/5kh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kh0 RCSB], [http://www.ebi.ac.uk/pdbsum/5kh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh0 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=5kh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh0 OCA], [http://pdbe.org/5kh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kh0 RCSB], [http://www.ebi.ac.uk/pdbsum/5kh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | [FeFe] hydrogenase (HydA) catalyzes interconversion between 2H+ and H2 at an active site composed of a [4Fe-4S] cluster linked to a 2Fe subcluster that harbors CO, CN- and azapropanedithiolate (adt2-) ligands. HydE, HydG and HydF are the maturases specifically involved in the biosynthesis of the 2Fe subcluster. Using ligands synthesized by HydE and HydG, HydF assembles a di-iron precursor of the 2Fe subcluster and transfers it to HydA for maturation. Here we report the first X-ray structure of HydF with its [4Fe-4S] cluster. The cluster is chelated by three cysteines and an exchangeable glutamate, which allows the binding of synthetic mimics of the 2Fe subcluster. [Fe2(adt)(CO)4(CN)2]2- is proposed to be the true di-iron precursor because, when bound to HydF, it matures HydA and displays features in Fourier transform infrared (FTIR) spectra that are similar to those of the native HydF active intermediate. A new route toward the generation of artificial hydrogenases, as combinations of HydF and such biomimetic complexes, is proposed on the basis of the observed hydrogenase activity of chemically modified HydF. | ||
+ | |||
+ | Structural and functional characterization of the hydrogenase-maturation HydF protein.,Caserta G, Pecqueur L, Adamska-Venkatesh A, Papini C, Roy S, Artero V, Atta M, Reijerse E, Lubitz W, Fontecave M Nat Chem Biol. 2017 Jul;13(7):779-784. doi: 10.1038/nchembio.2385. Epub 2017 May , 29. PMID:28553946<ref>PMID:28553946</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5kh0" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 10:11, 3 August 2017
Crystal Structure of HydF from thermosipho melanesiensis in complex with a [4Fe-4S] cluster
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