1by3

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{{STRUCTURE_1by3| PDB=1by3 | SCENE= }}
{{STRUCTURE_1by3| PDB=1by3 | SCENE= }}
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'''FHUA FROM E. COLI'''
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===FHUA FROM E. COLI===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Ligand-gated]]
[[Category: Ligand-gated]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:54:12 2008''

Revision as of 16:54, 30 June 2008

Image:1by3.png

Template:STRUCTURE 1by3

FHUA FROM E. COLI

Template:ABSTRACT PUBMED 9865695

About this Structure

1BY3 is a Single protein structure of sequence from Escherichia coli. 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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