2fcp

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[[Image:2fcp.jpg|left|200px]]
[[Image:2fcp.jpg|left|200px]]
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{{Structure
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|PDB= 2fcp |SIZE=350|CAPTION= <scene name='initialview01'>2fcp</scene>, resolution 2.50&Aring;
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{{STRUCTURE_2fcp| PDB=2fcp | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcp OCA], [http://www.ebi.ac.uk/pdbsum/2fcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fcp RCSB]</span>
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'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI'''
'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI'''
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[[Category: Hofmann, E.]]
[[Category: Hofmann, E.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: active transport]]
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[[Category: Active transport]]
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[[Category: ferrichrome-iron receptor]]
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[[Category: Ferrichrome-iron receptor]]
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[[Category: integral outer membrane protein]]
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[[Category: Integral outer membrane protein]]
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[[Category: iron transport protein]]
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[[Category: Iron transport protein]]
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[[Category: tonb-dependent receptor]]
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[[Category: Tonb-dependent receptor]]
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Revision as of 00:44, 4 May 2008

Template:STRUCTURE 2fcp

FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI


Overview

FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta sheet and four short alpha helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.

About this Structure

2FCP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide., Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W, Science. 1998 Dec 18;282(5397):2215-20. PMID:9856937 Page seeded by OCA on Sun May 4 03:44:22 2008

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