1by5
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(New page: 200px<br /><applet load="1by5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by5, resolution 2.60Å" /> '''FHUA FROM E. COLI, W...)
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Revision as of 09:53, 20 November 2007
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FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME
Overview
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.
About this Structure
1BY5 is a Single protein structure of sequence from Escherichia coli and Ustilago sphaerogena with FE and OES as ligands. Full crystallographic information is available from OCA.
Reference
Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes., Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, Moras D, Cell. 1998 Dec 11;95(6):771-8. PMID:9865695
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