PMID:15488768

Citation	Matousek, WM and Alexandrescu, AT (2004) NMR structure of the C-terminal domain of SecA in the free state. Biochim. Biophys. Acta 1702:163-71
Abstract	SecA is an integral component of the prokaryotic Sec preprotein secretory translocase system. We report here the solution NMR structure of a fragment corresponding to the C-terminal domain of Escherichia coli SecA. In the presence of Zn2+, the fragment adopts a shortened version of the classic betabetaalpha zinc finger fold. The isolated C-terminal domain shows substantial differences from the X-ray structure of a homologous SecA domain bound to the chaperone-like cofactor SecB. The differences between the structures of the free and bound forms suggest that binding to SecB causes a perturbation of the C-terminal domain's intrinsically favored betabetaalpha fold.
Links	PubMed Online version:10.1016/j.bbapap.2004.08.012
Keywords	Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/genetics; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Protein Structure, Secondary; Sequence Alignment; Zinc/chemistry; Zinc Fingers
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