1kmo

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{{STRUCTURE_1kmo| PDB=1kmo | SCENE= }}
{{STRUCTURE_1kmo| PDB=1kmo | SCENE= }}
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'''Crystal structure of the Outer Membrane Transporter FecA'''
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===Crystal structure of the Outer Membrane Transporter FecA===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 11872840 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11872840}}
==About this Structure==
==About this Structure==
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[[Category: Siderophore]]
[[Category: Siderophore]]
[[Category: Tonb-dependent receptor]]
[[Category: Tonb-dependent receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:33:53 2008''

Revision as of 07:33, 2 July 2008

Image:1kmo.png

Template:STRUCTURE 1kmo

Crystal structure of the Outer Membrane Transporter FecA

Template:ABSTRACT PUBMED 11872840

About this Structure

1KMO is a Single protein structure of sequence from Escherichia coli. 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

Page seeded by OCA on Wed Jul 2 10:33:53 2008

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