2fcp

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[[Image:2fcp.png|left|200px]]
 
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{{STRUCTURE_2fcp| PDB=2fcp | SCENE= }}
{{STRUCTURE_2fcp| PDB=2fcp | SCENE= }}
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===FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI===
===FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI===
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{{ABSTRACT_PUBMED_9856937}}
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==Function==
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[[http://www.uniprot.org/uniprot/FHUA_ECOLI FHUA_ECOLI]] This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin.<ref>PMID:8617231</ref>
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:009856937</ref><references group="xtra"/>
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<ref group="xtra">PMID:009856937</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Diederichs, K.]]
[[Category: Diederichs, K.]]

Revision as of 08:12, 23 April 2014

Template:STRUCTURE 2fcp

Contents

FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI

Template:ABSTRACT PUBMED 9856937

Function

[FHUA_ECOLI] This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin.[1]

About this Structure

2fcp is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 1998 Dec 18;282(5397):2215-20. PMID:9856937
  1. ↑ Bonhivers M, Ghazi A, Boulanger P, Letellier L. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. EMBO J. 1996 Apr 15;15(8):1850-6. PMID:8617231

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