View source for 5xvb


==[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in an H2-reduced condition==
<StructureSection load='5xvb' size='340' side='right'caption='[[5xvb]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xvb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_sp._S-77 Citrobacter sp. S-77]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XVB 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]] 1.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</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=5xvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xvb OCA], [https://pdbe.org/5xvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xvb RCSB], [https://www.ebi.ac.uk/pdbsum/5xvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xvb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3B6UEQ0_9ENTR A0A3B6UEQ0_9ENTR] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.[ARBA:ARBA00059419]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe-4S] cluster proximal to the Ni-Fe active site. The presence of relocatable water molecules and a flexible aspartate enables the [4Fe-4S] to display redox-dependent conformational changes. These structural features are proposed to be the key aspects that protect the active site from O2 attack.

Redox-dependent conformational changes of a proximal [4Fe-4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2.,Noor NDM, Matsuura H, Nishikawa K, Tai H, Hirota S, Kim J, Kang J, Tateno M, Yoon KS, Ogo S, Kubota S, Shomura Y, Higuchi Y Chem Commun (Camb). 2018 Oct 30;54(87):12385-12388. doi: 10.1039/c8cc06261g. PMID:30328414<ref>PMID:30328414</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xvb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Citrobacter sp. S-77]]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Hirota S]]
[[Category: Kang J]]
[[Category: Kim J]]
[[Category: Matsuura H]]
[[Category: Muhd Noor ND]]
[[Category: Nishikawa K]]
[[Category: Ogo S]]
[[Category: Shomura Y]]
[[Category: Tai H]]
[[Category: Tateno M]]
[[Category: Yoon KS]]