This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fx3
From Proteopedia
|
CRYSTAL STRUCTURE OF H. INFLUENZAE SECB
Overview
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.
About this Structure
1FX3 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 15:25:06 2007
