9cu1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Azotobacter vinelandii filamentous 2:2:1 MoFeP:FeP:FeSII-Complex (termini; C1 symmetry)== | |
| - | + | <StructureSection load='9cu1' size='340' side='right'caption='[[9cu1]], [[Resolution|resolution]] 2.83Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9cu1]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CU1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.83Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9cu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cu1 OCA], [https://pdbe.org/9cu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cu1 RCSB], [https://www.ebi.ac.uk/pdbsum/9cu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cu1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FESII_AZOVI FESII_AZOVI] Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:10220344, PubMed:26654855, PubMed:7548055, PubMed:7830548). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).<ref>PMID:10220344</ref> <ref>PMID:26654855</ref> <ref>PMID:7548055</ref> <ref>PMID:7830548</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Britt RD]] | ||
| + | [[Category: Cook BD]] | ||
| + | [[Category: Eng VH]] | ||
| + | [[Category: Herzik MA]] | ||
| + | [[Category: Narehood SM]] | ||
| + | [[Category: Shiau A]] | ||
| + | [[Category: Srisantitham S]] | ||
| + | [[Category: Tezcan FA]] | ||
Current revision
Azotobacter vinelandii filamentous 2:2:1 MoFeP:FeP:FeSII-Complex (termini; C1 symmetry)
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