2fcp
From Proteopedia
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|PDB= 2fcp |SIZE=350|CAPTION= <scene name='initialview01'>2fcp</scene>, resolution 2.50Å | |PDB= 2fcp |SIZE=350|CAPTION= <scene name='initialview01'>2fcp</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AAE:ACETOACETIC+ACID'>AAE</scene>, <scene name='pdbligand=EA2:AMINOETHANOLPYROPHOSPHATE'>EA2</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=GP1:GLUCOSAMINE+1-PHOSPHATE'>GP1</scene>, <scene name='pdbligand=GP4:GLUCOSAMINE+4-PHOSPHATE'>GP4</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=LIL:2-TRIDECANOYLOXY-PENTADECANOIC+ACID'>LIL</scene>, <scene name='pdbligand=LIM:3-OXO-PENTADECANOIC+ACID'>LIM</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Hofmann, E.]] | [[Category: Hofmann, E.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
| - | [[Category: AAE]] | ||
| - | [[Category: EA2]] | ||
| - | [[Category: LIL]] | ||
| - | [[Category: LIM]] | ||
| - | [[Category: NI]] | ||
| - | [[Category: PO4]] | ||
[[Category: active transport]] | [[Category: active transport]] | ||
[[Category: ferrichrome-iron receptor]] | [[Category: ferrichrome-iron receptor]] | ||
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[[Category: tonb-dependent receptor]] | [[Category: tonb-dependent receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:01:00 2008'' |
Revision as of 00:01, 31 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | , , , , , , , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 03:01:00 2008
