9cu1: Difference between revisions
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==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]] | |||
Latest revision as of 06:18, 15 January 2025
Azotobacter vinelandii filamentous 2:2:1 MoFeP:FeP:FeSII-Complex (termini; C1 symmetry)
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