1FI1

FhuA in complex with lipopolysaccharide and rifamycin CGP4832

Summary for 1FI1

• Entry DOI: 10.2210/pdb1fi1/pdb
• Related: 1QFF 1QFG 1fcp 1qjq 1qkc 2fcp
• Descriptor: FERRICHROME-IRON RECEPTOR, DECYLAMINE-N,N-DIMETHYL-N-OXIDE, alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose-(1-3)-[L-glycero-alpha-D-manno-heptopyranose-(1-7)]L-glycero-alpha-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-2,3-dideoxy-alpha-D-glucoyranose-(1-6)-2-amino-2-deoxy-alpha-D-glucopyranose, ... (11 entities in total)
• Functional Keywords: outer membrane protein; tonb-dependent receptor; fhua; siderophore receptor; integral membrane protein; lipopolysaccharide; rifamycin cgp 4832; beta-barrel; antibiotic, metal transport
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 83467.26

Authors

Ferguson, A.D.,Koedding, J.,Boes, C.,Walker, G.,Coulton, J.W.,Diederichs, K.,Braun, V.,Welte, W. (deposition date: 2000-08-03, release date: 2001-08-29, Last modification date: 2022-12-21)

Primary citation

Ferguson, A.D.,Kodding, J.,Walker, G.,Bos, C.,Coulton, J.W.,Diederichs, K.,Braun, V.,Welte, W.
Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA.
Structure, 9:707-716, 2001

PubMed Abstract: FhuA, an integral membrane protein of Escherichia coli, actively transports ferrichrome and the structurally related antibiotic albomycin across the outer membrane. The transport is coupled to the proton motive force, which energizes FhuA through the inner-membrane protein TonB. FhuA also transports the semisynthetic rifamycin derivative CGP 4832, although the chemical structure of this antibiotic differs markedly from that of ferric hydroxamates.

PubMed: 11587645
DOI: 10.1016/S0969-2126(01)00631-1

Experimental method

X-RAY DIFFRACTION (2.9 Å)