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- Title
Structural determinants of SecB recognition by SecA in bacterial protein translocation.
- Authors
Zhou, Jiahai; Xu, Zhaohui
- 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.
- Subjects
BACTERIA; PROTEINS; ADENOSINE triphosphate; ADENOSINE triphosphatase
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 11, p942
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb980