2min

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(New page: 200px<br /><applet load="2min" size="450" color="white" frame="true" align="right" spinBox="true" caption="2min, resolution 2.03&Aring;" /> '''NITROGENASE MOFE PRO...)
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[[Image:2min.gif|left|200px]]<br /><applet load="2min" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2min, resolution 2.03&Aring;" />
 
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'''NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE'''<br />
 
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==Overview==
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==NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE==
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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.
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<StructureSection load='2min' size='340' side='right'caption='[[2min]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2min]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1min 1min]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MIN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2min FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2min OCA], [https://pdbe.org/2min PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2min RCSB], [https://www.ebi.ac.uk/pdbsum/2min PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2min ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NIFD_AZOVI NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/2min_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2min ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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].
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*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9063865 9063865]
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Nitrogenase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Day MW]]
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[[Category: Day, M.W.]]
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[[Category: Kim J]]
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[[Category: Kim, J.]]
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[[Category: Peters JW]]
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[[Category: Peters, J.W.]]
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[[Category: Rees DC]]
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[[Category: Rees, D.C.]]
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[[Category: Soltis SM]]
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[[Category: Soltis, S.M.]]
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[[Category: Stowell MHB]]
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[[Category: Stowell, M.H.B.]]
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[[Category: CA]]
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[[Category: CFM]]
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[[Category: CLF]]
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[[Category: HCA]]
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[[Category: biological nitrogen fixation]]
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[[Category: molybdoenzymes]]
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[[Category: nitrogen fixation]]
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[[Category: nitrogen metabolism]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:45:05 2007''
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Current revision

NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE

PDB ID 2min

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