2hdi
From Proteopedia
Crystal structure of the Colicin I receptor Cir from E.coli in complex with receptor binding domain of Colicin Ia.
Structural highlights
FunctionCIRA_ECOLI Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. 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 PubMedColicin 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. 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 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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