1ozb
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(New page: 200px<br /><applet load="1ozb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ozb, resolution 2.80Å" /> '''Crystal Structure of...)
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Revision as of 21:11, 20 November 2007
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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 ZN 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
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