1fx3

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spinqualitylabelsall models 1fx3, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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