PMID:9781695
| Citation |
Shilton, B, Svergun, DI, Volkov, VV, Koch, MH, Cusack, S and Economou, A (1998) Escherichia coli SecA shape and dimensions. FEBS Lett. 436:277-82 |
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| Abstract |
SecA shape and conformational flexibility in solution were studied by small angle X-ray scattering. Dimeric SecA is a very elongated molecule, 15 nm long and 8 nm wide. SecA is therefore four times as long as the membrane is wide. The two globular protomers are distinctly separated and share limited surface of intermolecular contacts. ATP, ADP or adenylyl-imidodiphosphate (AMP-PNP) binding does not alter the SecA radius of gyration. A SecA mutant that catalyzes multiple rounds of ATP hydrolysis does not undergo conformational changes detectable by small angle X-ray scattering (SAXS). We conclude that SecA conformational alterations observed biochemically during nucleotide interaction are only small-scale and localized. The ramifications of these findings on SecA/SecYEG interaction are discussed. |
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| Keywords |
Adenosine Diphosphate/metabolism; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Adenylyl Imidodiphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Dimerization; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Transport Proteins; Models, Molecular; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Scattering, Radiation; Solutions; X-Ray Diffraction/methods; X-Rays |
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