2hdf

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==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17464289 17464289]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17464289 17464289]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Buchanan, S.K.]]
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[[Category: Buchanan, S K.]]
[[Category: Esser, L.]]
[[Category: Esser, L.]]
[[Category: Lukacik, P.]]
[[Category: Lukacik, P.]]
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[[Category: tonb box]]
[[Category: tonb box]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:03:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:49 2008''

Revision as of 15:40, 21 February 2008


2hdf, resolution 2.65Å

Drag the structure with the mouse to rotate

Crystal structure of the Colicin I receptor Cir from E.coli

Overview

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 Structure

2HDF is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

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

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