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==[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant C299D==
==[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant C299D==
<StructureSection load='6glz' size='340' side='right' caption='[[6glz]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
<StructureSection load='6glz' size='340' side='right'caption='[[6glz]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6glz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GLZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[6glz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GLZ 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xdc|4xdc]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6glz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6glz OCA], [https://pdbe.org/6glz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6glz RCSB], [https://www.ebi.ac.uk/pdbsum/6glz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6glz 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=6glz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6glz OCA], [http://pdbe.org/6glz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6glz RCSB], [http://www.ebi.ac.uk/pdbsum/6glz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6glz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA]
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6glz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ferredoxin hydrogenase]]
[[Category: Clostridium pasteurianum]]
[[Category: Duan, J]]
[[Category: Large Structures]]
[[Category: Esselborn, J]]
[[Category: Duan J]]
[[Category: Happe, T]]
[[Category: Esselborn J]]
[[Category: Hofmann, E]]
[[Category: Happe T]]
[[Category: Winkler, M]]
[[Category: Hofmann E]]
[[Category: H-cluster]]
[[Category: Winkler M]]
[[Category: Hydrogenase]]
[[Category: Oxidoreductase]]
[[Category: Semisynthetic enzyme]]
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