View source for 5xfa


==Crystal structure of NAD+-reducing [NiFe]-hydrogenase in the H2-reduced state==
<StructureSection load='5xfa' size='340' side='right'caption='[[5xfa]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xfa]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenophilus_thermoluteolus Hydrogenophilus thermoluteolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XFA 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=5xfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfa OCA], [https://pdbe.org/5xfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xfa RCSB], [https://www.ebi.ac.uk/pdbsum/5xfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A077L6X8_HYDTE A0A077L6X8_HYDTE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NAD+ (oxidized form of NAD:nicotinamide adenine dinucleotide)-reducing soluble [NiFe]-hydrogenase (SH) is phylogenetically related to NADH (reduced form of NAD+):quinone oxidoreductase (complex I), but the geometrical arrangements of the subunits and Fe-S clusters are unclear. Here, we describe the crystal structures of SH in the oxidized and reduced states. The cluster arrangement is similar to that of complex I, but the subunits orientation is not, which supports the hypothesis that subunits evolved as prebuilt modules. The oxidized active site includes a six-coordinate Ni, which is unprecedented for hydrogenases, whose coordination geometry would prevent O2 from approaching. In the reduced state showing the normal active site structure without a physiological electron acceptor, the flavin mononucleotide cofactor is dissociated, which may be caused by the oxidation state change of nearby Fe-S clusters and may suppress production of reactive oxygen species.

Structural basis of the redox switches in the NAD+-reducing soluble [NiFe]-hydrogenase.,Shomura Y, Taketa M, Nakashima H, Tai H, Nakagawa H, Ikeda Y, Ishii M, Igarashi Y, Nishihara H, Yoon KS, Ogo S, Hirota S, Higuchi Y Science. 2017 Sep 1;357(6354):928-932. doi: 10.1126/science.aan4497. PMID:28860386<ref>PMID:28860386</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xfa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hydrogenophilus thermoluteolus]]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Hirota S]]
[[Category: Igarashi Y]]
[[Category: Ikeda Y]]
[[Category: Ishii M]]
[[Category: Nakagawa H]]
[[Category: Nakashima H]]
[[Category: Nishihara H]]
[[Category: Ogo S]]
[[Category: Shomura Y]]
[[Category: Tai H]]
[[Category: Taketa M]]
[[Category: Yoon KS]]