2min
From Proteopedia
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|PDB= 2min |SIZE=350|CAPTION= <scene name='initialview01'>2min</scene>, resolution 2.03Å | |PDB= 2min |SIZE=350|CAPTION= <scene name='initialview01'>2min</scene>, resolution 2.03Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFM:FE-MO-S+CLUSTER'>CFM</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2min FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2min OCA], [http://www.ebi.ac.uk/pdbsum/2min PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2min RCSB]</span> | ||
}} | }} | ||
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[[Category: Soltis, S M.]] | [[Category: Soltis, S M.]] | ||
[[Category: Stowell, M H.B.]] | [[Category: Stowell, M H.B.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CFM]] | ||
| - | [[Category: CLF]] | ||
| - | [[Category: HCA]] | ||
[[Category: biological nitrogen fixation]] | [[Category: biological nitrogen fixation]] | ||
[[Category: molybdoenzyme]] | [[Category: molybdoenzyme]] | ||
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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 04:04:11 2008'' |
Revision as of 01:04, 31 March 2008
| |||||||
| , resolution 2.03Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE
Overview
The structure of the nitrogenase MoFe-protein from Azotobacter vinelandii has been refined to 2.0 A resolution in two oxidation states. EPR studies on the crystals indicate that the structures correspond to the spectroscopically assigned oxidized (P(OX)/M(OX)) and the native or dithionite-reduced (P(N)/M(N)) forms of the enzyme. Both MoFe-protein structures are essentially identical, with the exception of the P-cluster. The MoFe-protein P-cluster in each state is found to contain eight Fe and seven S atoms. Interconversion between the two redox states involves movement of two Fe atoms and an exchange of protein coordination for ligands supplied by a central S atom. In the oxidized P(OX) state, the cluster is coordinated by the protein through six cysteine ligands, Ser-beta188 O gamma, and the backbone amide of Cys-alpha88. In the native P(N) state, Ser-beta188 O gamma and the amide N of Cys-alpha88 no longer coordinate the cluster due to movement of their coordinated Fe atoms toward the central sulfur. Consequently, this central sulfur adopts a distorted octahedral environment with six surrounding Fe atoms. A previously described model of the P-cluster containing 8Fe-8S likely reflects the inappropriate modeling of a single structure to a mixture of these two P-cluster redox states. These observed redox-mediated structural changes of the P-cluster suggest a role for this cluster in coupling electron transfer and proton transfer in nitrogenase.
About this Structure
2MIN is a Protein complex structure of sequences from Azotobacter vinelandii. This structure supersedes the now removed PDB entry 1MIN. Full crystallographic information is available from OCA.
Reference
Redox-dependent structural changes in the nitrogenase P-cluster., Peters JW, Stowell MH, Soltis SM, Finnegan MG, Johnson MK, Rees DC, Biochemistry. 1997 Feb 11;36(6):1181-7. PMID:9063865
Page seeded by OCA on Mon Mar 31 04:04:11 2008
