1BY3

FHUA FROM E. COLI

Summary for 1BY3

• Entry DOI: 10.2210/pdb1by3/pdb
• Descriptor: PROTEIN (FERRICHROME-IRON RECEPTOR PRECURSOR (FHUA)), N-OCTYL-2-HYDROXYETHYL SULFOXIDE (3 entities in total)
• Functional Keywords: fhua, membrane protein, ligand-gated, iron transport
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P06971
• Total number of polymer chains: 1
• Total formula weight: 80373.43

Authors

Locher, K.P.,Rees, B.,Koebnik, R.,Mitschler, A.,Moulinier, L.,Rosenbusch, J.P.,Moras, D. (deposition date: 1998-10-22, release date: 1999-01-13, Last modification date: 2024-11-13)

Primary citation

Locher, K.P.,Rees, B.,Koebnik, R.,Mitschler, A.,Moulinier, L.,Rosenbusch, J.P.,Moras, D.
Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes.
Cell(Cambridge,Mass.), 95:771-778, 1998

PubMed Abstract: FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the presence and absence of ferrichrome. The monomeric protein consists of a hollow, 22-stranded, antiparallel beta barrel (residues 160-714), which is obstructed by a plug (residues 19-159). The binding site of ferrichrome, an aromatic pocket near the cell surface, undergoes minor changes upon association with the ligand. These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face. Our findings reveal the mechanism of signal transmission and suggest how the energy-transducing TonB complex senses ligand binding.

PubMed: 9865695
DOI: 10.1016/S0092-8674(00)81700-6

Experimental method

X-RAY DIFFRACTION (2.74 Å)