1n2c
From Proteopedia
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , and | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE
Overview
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.
About this Structure
1N2C is a Protein complex structure of sequences from Azotobacter vinelandii. The following page contains interesting information on the relation of 1N2C with [Nitrogenase]. Full crystallographic information is available from OCA.
Reference
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction., Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC, Nature. 1997 May 22;387(6631):370-6. PMID:9163420
Page seeded by OCA on Thu Mar 20 12:51:13 2008
Categories: Azotobacter vinelandii | Nitrogenase | Protein complex | Kisker, C. | Rees, D C. | Schindelin, H. | ADP | ALF | CA | CFM | CLF | HCA | MG | SF4 | Atp hydrolysis | Complex of nitrogenase protein | Electron transfer | Nitrogen fixation | Signal transduction
