2afh
From Proteopedia
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|PDB= 2afh |SIZE=350|CAPTION= <scene name='initialview01'>2afh</scene>, resolution 2.10Å | |PDB= 2afh |SIZE=350|CAPTION= <scene name='initialview01'>2afh</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFN:FE(7)-MO-S(9)-N+CLUSTER'>CFN</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2afi|2AFI]], [[2afk|2AFK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afh OCA], [http://www.ebi.ac.uk/pdbsum/2afh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2afh RCSB]</span> | ||
}} | }} | ||
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[[Category: Tezcan, F A.]] | [[Category: Tezcan, F A.]] | ||
[[Category: Walton, M Y.]] | [[Category: Walton, M Y.]] | ||
| - | [[Category: 1PE]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CFN]] | ||
| - | [[Category: CLF]] | ||
| - | [[Category: HCA]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: P6G]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: PG4]] | ||
| - | [[Category: PGE]] | ||
| - | [[Category: SF4]] | ||
| - | [[Category: TRS]] | ||
[[Category: iron-sulfur]] | [[Category: iron-sulfur]] | ||
[[Category: metal-binding]] | [[Category: metal-binding]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:00 2008'' |
Revision as of 22:52, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , , , , , | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Related: | 2AFI, 2AFK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Nucleotide-Free Av2-Av1 Complex
Overview
Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.
About this Structure
2AFH is a Protein complex structure of sequences from Azotobacter vinelandii. Full crystallographic information is available from OCA.
Reference
Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:16123301
Page seeded by OCA on Mon Mar 31 01:52:00 2008
