2afh

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[[Image:2afh.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Nucleotide-Free Av2-Av1 Complex==
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|PDB= 2afh |SIZE=350|CAPTION= <scene name='initialview01'>2afh</scene>, resolution 2.10&Aring;
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<StructureSection load='2afh' size='340' side='right'caption='[[2afh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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<table><tr><td colspan='2'>[[2afh]] is a 6 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=2AFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AFH FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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}}
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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=2afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afh OCA], [https://pdbe.org/2afh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2afh RCSB], [https://www.ebi.ac.uk/pdbsum/2afh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2afh 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/af/2afh_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=2afh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.
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'''Crystal Structure of Nucleotide-Free Av2-Av1 Complex'''
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Nitrogenase complexes: multiple docking sites for a nucleotide switch protein.,Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC Science. 2005 Aug 26;309(5739):1377-80. PMID:16123301<ref>PMID:16123301</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2afh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.
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*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2AFH 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=2AFH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16123301 16123301]
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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: Howard JB]]
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[[Category: Howard, J B.]]
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[[Category: Kaiser JT]]
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[[Category: Kaiser, J T.]]
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[[Category: Mustafi D]]
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[[Category: Mustafi, D.]]
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[[Category: Rees DC]]
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[[Category: Rees, D C.]]
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[[Category: Tezcan FA]]
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[[Category: Tezcan, F A.]]
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[[Category: Walton MY]]
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[[Category: Walton, M Y.]]
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[[Category: 1PE]]
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[[Category: CA]]
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[[Category: CFN]]
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[[Category: CLF]]
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[[Category: HCA]]
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[[Category: NA]]
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[[Category: P6G]]
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[[Category: PEG]]
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[[Category: PG4]]
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[[Category: PGE]]
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[[Category: SF4]]
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[[Category: TRS]]
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[[Category: iron-sulfur]]
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[[Category: metal-binding]]
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[[Category: molybdenum]]
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[[Category: nitrogen fixation]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:49:02 2008''
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Current revision

Crystal Structure of Nucleotide-Free Av2-Av1 Complex

PDB ID 2afh

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