Characterization of the Escherichia coli SecA Signal Peptide-Binding Site
نویسندگان
چکیده
منابع مشابه
Characterization of the Escherichia coli SecA signal peptide-binding site.
SecA signal peptide interaction is critical for initiating protein translocation in the bacterial Sec-dependent pathway. Here, we have utilized the recent nuclear magnetic resonance (NMR) and Förster resonance energy transfer studies that mapped the location of the SecA signal peptide-binding site to design and isolate signal peptide-binding-defective secA mutants. Biochemical characterization ...
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متن کاملEscherichia coli SecA shape and dimensions.
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...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2012
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.06150-11