2min: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2min" size="450" color="white" frame="true" align="right" spinBox="true" caption="2min, resolution 2.03Å" /> '''NITROGENASE MOFE PRO...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2min.gif|left|200px]]<br /><applet load="2min" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2min.gif|left|200px]]<br /><applet load="2min" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2min, resolution 2.03&Aring;" />
caption="2min, resolution 2.03&Aring;" />
'''NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE'''<br />
'''NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE'''<br />


==Overview==
==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.
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==
==About this Structure==
2MIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with CA, HCA, CLF and CFM as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1MIN. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MIN OCA].  
2MIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CLF:'>CLF</scene> and <scene name='pdbligand=CFM:'>CFM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1MIN. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MIN OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Day, M.W.]]
[[Category: Day, M W.]]
[[Category: Kim, J.]]
[[Category: Kim, J.]]
[[Category: Peters, J.W.]]
[[Category: Peters, J W.]]
[[Category: Rees, D.C.]]
[[Category: Rees, D C.]]
[[Category: Soltis, S.M.]]
[[Category: Soltis, S M.]]
[[Category: Stowell, M.H.B.]]
[[Category: Stowell, M H.B.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CFM]]
[[Category: CFM]]
Line 30: Line 30:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:45:05 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:43 2008''