1FEP

FERRIC ENTEROBACTIN RECEPTOR

Summary for 1FEP

• Entry DOI: 10.2210/pdb1fep/pdb
• Descriptor: FERRIC ENTEROBACTIN RECEPTOR (2 entities in total)
• Functional Keywords: outer membrane, iron transport, transport, tonb, receptor, membrane protein
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 80363.56

Authors

Buchanan, S.K.,Smith, B.S.,Ventatramani, L.,Xia, D.,Esser, L.,Palnitkar, M.,Chakraborty, R.,Van Der Helm, D.,Deisenhofer, J. (deposition date: 1998-11-24, release date: 1999-01-13, Last modification date: 2024-11-06)

Primary citation

Buchanan, S.K.,Smith, B.S.,Venkatramani, L.,Xia, D.,Esser, L.,Palnitkar, M.,Chakraborty, R.,van der Helm, D.,Deisenhofer, J.
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Nat.Struct.Biol., 6:56-63, 1999

PubMed Abstract: Integral outer membrane receptors for iron chelates and vitamin B12 carry out specific ligand transport against a concentration gradient. Energy for active transport is obtained from the proton-motive force of the inner membrane through physical interaction with TonB-ExbB-ExbD, an inner membrane complex. Here we report the crystal structure of an active transport, outer membrane receptor at 2.4 A resolution. Two distinct functional domains are revealed: (i) a 22-stranded beta-barrel that spans the outer membrane and contains large extracellular loops which appear to function in ligand binding; and (ii) a globular N-terminal domain that folds into the barrel pore, inhibiting access to the periplasm and contributing two additional loops for potential ligand binding. These loops could provide a signaling pathway between the processes of ligand recognition and TonB-mediated transport. The blockage of the pore suggests that the N-terminal domain must undergo a conformational rearrangement to allow ligand transport into the periplasm.

PubMed: 9886293
DOI: 10.1038/4931

Experimental method

X-RAY DIFFRACTION (2.4 Å)