2hdf
Crystal structure of the Colicin I receptor Cir from E.coli
|
OverviewOverview
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli, cells by binding to a specific receptor in the outer membrane, colicin I, receptor (70 kDa), and subsequently translocating its channel forming, domain across the periplasmic space, where it inserts into the inner, membrane and forms a voltage-dependent ion channel. We determined crystal, structures of colicin I receptor alone and in complex with the receptor, binding domain of colicin Ia. The receptor undergoes large and unusual, conformational changes upon colicin binding, opening at the cell surface, and positioning the receptor binding domain of colicin Ia directly above, it. We modelled the interaction with full-length colicin Ia to show that, the channel forming domain is initially positioned 150 A above the cell, surface. Functional data using full-length colicin Ia show that colicin I, receptor is necessary for cell surface binding, and suggest that the, receptor participates in translocation of colicin Ia across the outer, membrane.
About this StructureAbout this Structure
2HDF is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import., Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L, EMBO J. 2007 Apr 26;. PMID:17464289
Page seeded by OCA on Wed Jan 23 15:03:15 2008