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| - | [[Image:2min.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2min| PDB=2min | SCENE= }} | | {{STRUCTURE_2min| PDB=2min | SCENE= }} |
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| - | '''NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE'''
| + | ===NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9063865}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9063865 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9063865}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nitrogen metabolism]] | | [[Category: Nitrogen metabolism]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:33:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:42:25 2008'' |
Revision as of 13:42, 27 July 2008
Template:STRUCTURE 2min
NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE
Template:ABSTRACT PUBMED 9063865
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 Sun Jul 27 16:42:25 2008
