4wza

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'''Unreleased structure'''
 
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The entry 4wza is ON HOLD until Paper Publication
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==Asymmetric Nucleotide Binding in the Nitrogenase Complex==
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<StructureSection load='4wza' size='340' side='right'caption='[[4wza]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4wza]] 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=4WZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZA 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]] 1.8995&#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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=4wza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wza OCA], [https://pdbe.org/4wza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wza RCSB], [https://www.ebi.ac.uk/pdbsum/4wza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wza 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The roles of ATP hydrolysis in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure. Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue. In this structure the two nucleotides are bound asymmetrically by the Fe-protein subunits connected to the two different MoFe-protein subunits. This binding mode suggests that ATP hydrolysis and phosphate release may proceed by a stepwise mechanism. Through the associated Fe-protein conformational changes, a stepwise mechanism is anticipated to prolong the lifetime of the Fe-protein-MoFe-protein complex and, in turn, could orchestrate the sequence of intracomplex ET required for substrate reduction.
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Authors: Tezcan, F.A., Kaiser, J.T., Howard, J.B., Rees, D.C.
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Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase.,Tezcan FA, Kaiser JT, Howard JB, Rees DC J Am Chem Soc. 2014 Dec 23. PMID:25522159<ref>PMID:25522159</ref>
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Description: Asymmetric Nucleotide Binding in the Nitrogenase Complex
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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 4wza" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Azotobacter vinelandii]]
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[[Category: Large Structures]]
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[[Category: Howard JB]]
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[[Category: Kaiser JT]]
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[[Category: Rees DC]]
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[[Category: Tezcan FA]]

Current revision

Asymmetric Nucleotide Binding in the Nitrogenase Complex

PDB ID 4wza

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