5xvc
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in a ferricyanide-oxidized condition== | |
+ | <StructureSection load='5xvc' size='340' side='right'caption='[[5xvc]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5xvc]] 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=5XVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XVC 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]] 2.05Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5xvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xvc OCA], [https://pdbe.org/5xvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xvc RCSB], [https://www.ebi.ac.uk/pdbsum/5xvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xvc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A3B6UEQ1_9ENTR A0A3B6UEQ1_9ENTR] | ||
+ | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5xvc" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: Muhd Noor | + | [[Category: Citrobacter sp. S-77]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Higuchi Y]] |
- | [[Category: | + | [[Category: Hirota S]] |
- | [[Category: | + | [[Category: Kang J]] |
- | [[Category: | + | [[Category: Kim J]] |
- | [[Category: | + | [[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]] |
Current revision
[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in a ferricyanide-oxidized condition
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Categories: Citrobacter sp. S-77 | Large Structures | Higuchi Y | Hirota S | Kang J | Kim J | Matsuura H | Muhd Noor ND | Nishikawa K | Ogo S | Shomura Y | Tai H | Tateno M | Yoon KS