PMID:14517549

Citation	Zhou, J and Xu, Z (2003) Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat. Struct. Biol. 10:942-7
Abstract	SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues. The crystal structure of SecB in complex with the C-terminal 27 amino acids of SecA from Haemophilus influenzae shows that the SecA peptide is structured as a CCCH zinc-binding motif. One SecB tetramer is bound by two SecA peptides, and the interface involves primarily salt bridges and hydrogen bonding interactions. The structure explains the importance of the zinc-binding motif and conserved residues at the C terminus of SecA in its high-affinity binding with SecB. It also suggests a model of SecB-SecA interaction and its implication for the mechanism of pre-protein transfer in bacterial protein translocation.
Links	PubMed Online version:10.1038/nsb980
Keywords	Adenosine Triphosphatases/metabolism; Amino Acid Motifs; Amino Acid Sequence; Bacteria/metabolism; Bacterial Proteins/metabolism; Binding Sites; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/metabolism; Molecular Sequence Data; Protein Structure, Tertiary; Protein Transport; Zinc/metabolism
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