Structural highlights
Function
[SECB_HAEIN] One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target.
Crystal structure of the bacterial protein export chaperone secB.,Xu Z, Knafels JD, Yoshino K Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:11101901[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Z, Knafels JD, Yoshino K. Crystal structure of the bacterial protein export chaperone secB. Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:11101901 doi:10.1038/82040
