6gm2: Difference between revisions
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==[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E282D== | ==[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E282D== | ||
<StructureSection load='6gm2' size='340' side='right' caption='[[6gm2]], [[Resolution|resolution]] 2.76Å' scene=''> | <StructureSection load='6gm2' size='340' side='right'caption='[[6gm2]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6gm2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GM2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6gm2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pasteurianus"_(winogradsky_1895)_lehmann_and_neumann_1907 "bacillus pasteurianus" (winogradsky 1895) lehmann and neumann 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GM2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xdc|4xdc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xdc|4xdc]]</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=6gm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gm2 OCA], [http://pdbe.org/6gm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gm2 RCSB], [http://www.ebi.ac.uk/pdbsum/6gm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gm2 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=6gm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gm2 OCA], [http://pdbe.org/6gm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gm2 RCSB], [http://www.ebi.ac.uk/pdbsum/6gm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gm2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The unmatched catalytic turnover rates of [FeFe]-hydrogenases require an exceptionally efficient proton-transfer (PT) pathway to shuttle protons as substrates or products between bulk water and catalytic center. For clostridial [FeFe]-hydrogenase CpI such a pathway has been proposed and analyzed, but mainly on a theoretical basis. Here, eleven enzyme variants of two different [FeFe]-hydrogenases (CpI and HydA1) with substitutions in the presumptive PT-pathway are examined kinetically, spectroscopically, and crystallographically to provide solid experimental proof for its role in hydrogen-turnover. Targeting key residues of the PT-pathway by site directed mutagenesis significantly alters the pH-activity profile of these variants and in presence of H2 their cofactor is trapped in an intermediate state indicative of precluded proton-transfer. Furthermore, crystal structures coherently explain the individual levels of residual activity, demonstrating e.g. how trapped H2O molecules rescue the interrupted PT-pathway. These features provide conclusive evidence that the targeted positions are indeed vital for catalytic proton-transfer. | |||
Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.,Duan J, Senger M, Esselborn J, Engelbrecht V, Wittkamp F, Apfel UP, Hofmann E, Stripp ST, Happe T, Winkler M Nat Commun. 2018 Nov 9;9(1):4726. doi: 10.1038/s41467-018-07140-x. PMID:30413719<ref>PMID:30413719</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6gm2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ferredoxin hydrogenase]] | [[Category: Ferredoxin hydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Duan, J]] | [[Category: Duan, J]] | ||
[[Category: Esselborn, J]] | [[Category: Esselborn, J]] | ||
Revision as of 12:55, 25 December 2019
[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E282D
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