1OZB

Crystal Structure of SecB complexed with SecA C-terminus

Summary for 1OZB

• Entry DOI: 10.2210/pdb1ozb/pdb
• Related: 1FX3 1M6N 1NL3
• Descriptor: Protein-export protein secB, Preprotein translocase secA subunit, ZINC ION (3 entities in total)
• Functional Keywords: zinc binding motif, protein-protein complex, protein transport
• Biological source: Haemophilus influenzae; More
• Cellular location: Cytoplasm: P44853; Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P43803
• Total number of polymer chains: 10
• Total formula weight: 159370.29

Authors

Zhou, J.,Xu, Z. (deposition date: 2003-04-08, release date: 2003-10-14, Last modification date: 2024-04-03)

Primary citation

Zhou, J.,Xu, Z.
Structural determinants of SecB recognition by SecA in bacterial protein translocation
NAT.STRUCT.BIOL., 10:942-947, 2003

PubMed 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.

PubMed: 14517549
DOI: 10.1038/nsb980

Experimental method

X-RAY DIFFRACTION (2.8 Å)