Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein
| Autor: | Douglas C. Rees, Mika Y. Walton, Debarshi Mustafi, F. Akif Tezcan, Jens T. Kaiser, James B. Howard |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Molybdoferredoxin Chemical Phenomena Protein Conformation Stereochemistry ATPase Crystallography X-Ray Catalysis Protein Structure Secondary Cofactor Electron Transport chemistry.chemical_compound Adenosine Triphosphate Oxidoreductase Nitrogenase Molecular motor Nucleotide Protein Structure Quaternary chemistry.chemical_classification Azotobacter vinelandii Binding Sites Multidisciplinary biology Chemistry Physical Hydrolysis Hydrogen Bonding Adenosine Diphosphate Protein Subunits chemistry Docking (molecular) biology.protein Crystallization Dimerization Oxidation-Reduction Adenosine triphosphate Protein Binding |
| Zdroj: | Science. 309:1377-1380 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1115653 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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