2FCP

FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI

Summary for 2FCP

• Entry DOI: 10.2210/pdb2fcp/pdb
• Descriptor: PROTEIN (FERRIC HYDROXAMATE UPTAKE RECEPTOR), alpha-D-galactopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose-(1-3)-4-O-phosphono-D-glycero-beta-D-manno-heptopyranose-(1-3)-L-glycero-alpha-D-manno-heptopyranose-(1-5)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)]3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-4-O-phosphono-alpha-D-glucopyranose-(1-6)-2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, NICKEL (II) ION, ... (8 entities in total)
• Functional Keywords: tonb-dependent receptor, integral outer membrane protein, ferrichrome-iron receptor, active transport, iron transport protein, membrane protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 83374.67

Authors

Hofmann, E.,Ferguson, A.D.,Diederichs, K.,Welte, W. (deposition date: 1998-10-15, release date: 1999-01-13, Last modification date: 2024-11-20)

Primary citation

Ferguson, A.D.,Hofmann, E.,Coulton, J.W.,Diederichs, K.,Welte, W.
Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide.
Science, 282:2215-2220, 1998

PubMed Abstract: 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.

PubMed: 9856937
DOI: 10.1126/science.282.5397.2215

Experimental method

X-RAY DIFFRACTION (2.5 Å)