1mio

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(New page: 200px<br /><applet load="1mio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mio, resolution 3.0&Aring;" /> '''X-RAY CRYSTAL STRUCTU...)
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[[Image:1mio.gif|left|200px]]<br /><applet load="1mio" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mio, resolution 3.0&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION==
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The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein, from Clostridium pasteurianum (Cp1) has been determined at 3.0-A, resolution by a combination of isomorphous replacement, molecular, replacement, and noncrystallographic symmetry averaging. The structure of, Cp1, including the two types of metal centers associated with the protein, (the FeMo-cofactor and the P-cluster pair), is similar to that previously, described for the MoFe-protein from Azotobacter vinelandii (Av1). Unique, features of the Cp1 structure arise from the presence of an approximately, 50-residue insertion in the alpha subunit and an approximately 50-residue, deletion in the beta subunit. As a consequence, the FeMo-cofactor is more, buried in Cp1 than in Av1, since the insertion is located on the surface, above the FeMo-cofactor. The location of this insertion near the putative, nitrogenase iron protein binding site provides a structural basis for the, observation that the nitrogenase proteins from C. pasteurianum have low, activity with complementary nitrogenase proteins isolated from other, organisms. Mechanistic implications of the Cp1 structure for substrate, entry/product release, substrate binding to the FeMo-cofactor, and, electron- and proton-transfer reactions of nitrogenase are discussed.
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<StructureSection load='1mio' size='340' side='right'caption='[[1mio]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mio]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIO 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]] 3&#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=CLP:FE-S+CLUSTER'>CLP</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=1mio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mio OCA], [https://pdbe.org/1mio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mio RCSB], [https://www.ebi.ac.uk/pdbsum/1mio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mio ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NIFD_CLOPA NIFD_CLOPA] 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/1mio_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=1mio 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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1MIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with CA, HCA, CFM and CLP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MIO 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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X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution., Kim J, Woo D, Rees DC, Biochemistry. 1993 Jul 20;32(28):7104-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8393705 8393705]
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[[Category: Clostridium pasteurianum]]
[[Category: Clostridium pasteurianum]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Kim, J.]]
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[[Category: Kim J]]
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[[Category: Rees, D.C.]]
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[[Category: Rees DC]]
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[[Category: Woo, D.]]
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[[Category: Woo D]]
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[[Category: CA]]
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[[Category: CFM]]
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[[Category: CLP]]
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[[Category: HCA]]
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[[Category: molybdenum-iron protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:26:24 2007''
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Current revision

X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION

PDB ID 1mio

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