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1ozb
From Proteopedia
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Crystal Structure of SecB complexed with SecA C-terminus
Overview
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.
About this Structure
1OZB is a Protein complex structure of sequences from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Structural determinants of SecB recognition by SecA in bacterial protein translocation., Zhou J, Xu Z, Nat Struct Biol. 2003 Nov;10(11):942-7. Epub 2003 Sep 28. PMID:14517549
Page seeded by OCA on Thu Feb 21 14:23:20 2008
