1KMO

Crystal structure of the Outer Membrane Transporter FecA

Summary for 1KMO

• Entry DOI: 10.2210/pdb1kmo/pdb
• Related: 1kmp
• Descriptor: Iron(III) dicitrate transport protein fecA, LAURYL DIMETHYLAMINE-N-OXIDE, HEPTANE-1,2,3-TRIOL, ... (4 entities in total)
• Functional Keywords: membrane protein, iron transporter, tonb-dependent receptor, siderophore
• Biological source: Escherichia coli K12
• Cellular location: Cell outer membrane: P13036
• Total number of polymer chains: 1
• Total formula weight: 89602.49

Authors

Ferguson, A.D.,Chakraborty, R.,Smith, B.S.,Esser, L.,van der Helm, D.,Deisenhofer, J. (deposition date: 2001-12-17, release date: 2002-03-06, Last modification date: 2024-02-14)

Primary citation

Ferguson, A.D.,Chakraborty, R.,Smith, B.S.,Esser, L.,van der Helm, D.,Deisenhofer, J.
Structural basis of gating by the outer membrane transporter FecA.
Science, 295:1715-1719, 2002

PubMed Abstract: Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.

PubMed: 11872840
DOI: 10.1126/science.1067313

Experimental method

X-RAY DIFFRACTION (2 Å)