2afh
From Proteopedia
(New page: 200px<br /><applet load="2afh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2afh, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:2afh.gif|left|200px]]<br /><applet load="2afh" size=" | + | [[Image:2afh.gif|left|200px]]<br /><applet load="2afh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2afh, resolution 2.10Å" /> | caption="2afh, resolution 2.10Å" /> | ||
'''Crystal Structure of Nucleotide-Free Av2-Av1 Complex'''<br /> | '''Crystal Structure of Nucleotide-Free Av2-Av1 Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2AFH 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, NA, HCA, CFN, CLF, SF4, TRS, PGE, PG4, P6G, 1PE and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 2AFH 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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CFN:'>CFN</scene>, <scene name='pdbligand=CLF:'>CLF</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=TRS:'>TRS</scene>, <scene name='pdbligand=PGE:'>PGE</scene>, <scene name='pdbligand=PG4:'>PG4</scene>, <scene name='pdbligand=P6G:'>P6G</scene>, <scene name='pdbligand=1PE:'>1PE</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Howard, J | + | [[Category: Howard, J B.]] |
| - | [[Category: Kaiser, J | + | [[Category: Kaiser, J T.]] |
[[Category: Mustafi, D.]] | [[Category: Mustafi, D.]] | ||
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
| - | [[Category: Tezcan, F | + | [[Category: Tezcan, F A.]] |
| - | [[Category: Walton, M | + | [[Category: Walton, M Y.]] |
[[Category: 1PE]] | [[Category: 1PE]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:52 2008'' |
Revision as of 14:26, 21 February 2008
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Crystal Structure of Nucleotide-Free Av2-Av1 Complex
Overview
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.
About this Structure
2AFH is a Protein complex structure of sequences from Azotobacter vinelandii with , , , , , , , , , , and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:26:52 2008
Categories: Azotobacter vinelandii | Nitrogenase | Protein complex | Howard, J B. | Kaiser, J T. | Mustafi, D. | Rees, D C. | Tezcan, F A. | Walton, M Y. | 1PE | CA | CFN | CLF | HCA | NA | P6G | PEG | PG4 | PGE | SF4 | TRS | Iron-sulfur | Metal-binding | Molybdenum | Nitrogen fixation | Oxidoreductase
