View source for 6n59


==1.0 Angstrom crystal structure of [FeFe]-hydrogenase==
<StructureSection load='6n59' size='340' side='right'caption='[[6n59]], [[Resolution|resolution]] 1.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6n59]] is a 1 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=6N59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N59 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.02&#8491;</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=GOL:GLYCEROL'>GOL</scene></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=6n59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n59 OCA], [https://pdbe.org/6n59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n59 RCSB], [https://www.ebi.ac.uk/pdbsum/6n59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n59 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interac-tions of the iron-sulfur containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe Clostridium pasteurianum produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable six orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicate that protein secondary interactions directly influence the relative stabiliza-tion/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias.

Tuning catalytic bias of hydrogen gas producing hydrogenases.,Artz JH, Zadvornyy OA, Mulder DW, Keable SM, Cohen AE, Ratzloff MW, Williams SG, Ginovska B, Kumar N, Song J, McPhillips SE, Davidson C, Lyubimov AY, Pence N, Schut GJ, Jones AK, Soltis SM, Adams M, Raugei S, King PW, Peters JW J Am Chem Soc. 2019 Dec 9. doi: 10.1021/jacs.9b08756. PMID:31816235<ref>PMID:31816235</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6n59" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium pasteurianum]]
[[Category: Large Structures]]
[[Category: Artz JH]]
[[Category: Keable SM]]
[[Category: Peters JW]]
[[Category: Zadvornyy OA]]