1m1n

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[[Image:1m1n.gif|left|200px]]
 
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==Nitrogenase MoFe protein from Azotobacter vinelandii==
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The line below this paragraph, containing "STRUCTURE_1m1n", creates the "Structure Box" on the page.
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<StructureSection load='1m1n' size='340' side='right'caption='[[1m1n]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m1n]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1N 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]] 1.16&#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=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></td></tr>
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{{STRUCTURE_1m1n| PDB=1m1n | SCENE= }}
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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=1m1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1n OCA], [https://pdbe.org/1m1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1n RCSB], [https://www.ebi.ac.uk/pdbsum/1m1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1n 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/m1/1m1n_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=1m1n ConSurf].
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<div style="clear:both"></div>
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'''Nitrogenase MoFe protein from Azotobacter vinelandii'''
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==See Also==
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*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.
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==About this Structure==
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1M1N is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1N OCA].
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==Reference==
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Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor., Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC, Science. 2002 Sep 6;297(5587):1696-700. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12215645 12215645]
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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: Andrade SLA]]
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[[Category: Andrade, S L.A.]]
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[[Category: Einsle O]]
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[[Category: Einsle, O.]]
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[[Category: Howard JB]]
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[[Category: Howard, J B.]]
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[[Category: Rees DC]]
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[[Category: Rees, D C.]]
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[[Category: Schmid B]]
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[[Category: Schmid, B.]]
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[[Category: Tezcan FA]]
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[[Category: Tezcan, F A.]]
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[[Category: Yoshida M]]
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[[Category: Yoshida, M.]]
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[[Category: Atomic resolution]]
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[[Category: Central nitrogen ligand]]
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[[Category: Femo cofactor]]
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[[Category: Nitrogen fixation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:31:31 2008''
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Current revision

Nitrogenase MoFe protein from Azotobacter vinelandii

PDB ID 1m1n

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