1kmo

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(New page: 200px<br /><applet load="1kmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmo, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1kmo.gif|left|200px]]<br /><applet load="1kmo" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kmo.gif|left|200px]]<br /><applet load="1kmo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kmo, resolution 2.00&Aring;" />
caption="1kmo, resolution 2.00&Aring;" />
'''Crystal structure of the Outer Membrane Transporter FecA'''<br />
'''Crystal structure of the Outer Membrane Transporter FecA'''<br />
==Overview==
==Overview==
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Siderophore-mediated acquisition systems facilitate iron uptake. We, present the crystallographic structure of the integral outer membrane, receptor FecA from Escherichia coli with and without ferric citrate at 2.5, and 2.0 angstrom resolution. FecA is composed of three distinct domains:, the barrel, plug, and NH2-terminal extension. Binding of ferric citrate, triggers a conformational change of the extracellular loops that close the, external pocket of FecA. Ligand-induced allosteric transitions are, propagated through the outer membrane by the plug domain, signaling the, occupancy of the receptor in the periplasm. These data establish the, structural basis of gating for receptors dependent on the cytoplasmic, membrane protein TonB. By compiling available data for this family of, receptors, we propose a mechanism for the energy-dependent transport of, siderophores.
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Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.
==About this Structure==
==About this Structure==
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1KMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with LDA and HTO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KMO OCA].
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1KMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=HTO:'>HTO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMO OCA].
==Reference==
==Reference==
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[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
[[Category: Esser, L.]]
[[Category: Esser, L.]]
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[[Category: Ferguson, A.D.]]
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[[Category: Ferguson, A D.]]
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[[Category: Helm, D.van.der.]]
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[[Category: Helm, D van der.]]
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[[Category: Smith, B.S.]]
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[[Category: Smith, B S.]]
[[Category: HTO]]
[[Category: HTO]]
[[Category: LDA]]
[[Category: LDA]]
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[[Category: tonb-dependent receptor]]
[[Category: tonb-dependent receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:22:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:46 2008''

Revision as of 11:35, 21 February 2008


1kmo, resolution 2.00Å

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Crystal structure of the Outer Membrane Transporter FecA

Overview

Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.

About this Structure

1KMO is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of gating by the outer membrane transporter FecA., Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, Deisenhofer J, Science. 2002 Mar 1;295(5560):1715-9. PMID:11872840

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