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1fcp
From Proteopedia
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'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON''' | '''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON''' | ||
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[[Category: Hofmann, E.]] | [[Category: Hofmann, E.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
| - | [[Category: | + | [[Category: Active transport]] |
| - | [[Category: | + | [[Category: Ferrichrome-iron receptor]] |
| - | [[Category: | + | [[Category: Integral outer membrane protein]] |
| - | [[Category: | + | [[Category: Iron transport protein]] |
| - | [[Category: | + | [[Category: Tonb-dependent receptor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:10:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:10, 2 May 2008
FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON
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
1FCP 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 Fri May 2 16:10:46 2008
