1xkh

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{{STRUCTURE_1xkh| PDB=1xkh | SCENE= }}
{{STRUCTURE_1xkh| PDB=1xkh | SCENE= }}
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'''Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine'''
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===Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine===
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==Overview==
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The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa translocates ferric-pyoverdine across the outer membrane via an energy consuming mechanism that involves the inner membrane energy transducing complex of TonB-ExbB-ExbD and the proton motive force. We solved the crystal structure of FpvA loaded with iron-free pyoverdine at 3.6 angstroms resolution. The pyoverdine receptor is folded in two domains: a transmembrane 22-stranded beta-barrel domain occluded by an N-terminal domain containing a mixed four-stranded beta-sheet (the plug). The beta-strands of the barrel are connected by long extracellular loops and short periplasmic turns. The iron-free pyoverdine is bound at the surface of the receptor in a pocket lined with aromatic residues while the extracellular loops do not completely cover the pyoverdine binding site. The TonB box, which is involved in intermolecular contacts with the TonB protein of the inner membrane, is observed in an extended conformation. Comparison of this first reported structure of an iron-siderophore transporter from a bacterium other than Escherichia coli with the known structures of the E.coli TonB-dependent transporters reveals a high structural homology and suggests that a common sensing mechanism exists for the iron-loading status in all bacterial iron siderophore transporters.
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The line below this paragraph, {{ABSTRACT_PUBMED_15733922}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15733922 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15733922}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution., Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F, J Mol Biol. 2005 Mar 18;347(1):121-34. Epub 2005 Jan 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15733922 15733922]
The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution., Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F, J Mol Biol. 2005 Mar 18;347(1):121-34. Epub 2005 Jan 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15733922 15733922]
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Crystallization and preliminary X-ray analysis of the outer membrane pyoverdine receptor FpvA from Pseudomonas aeruginosa., Cobessi D, Celia H, Folschweiller N, Heymann M, Schalk I, Abdallah M, Pattus F, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1467-9. Epub 2004, Jul 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15272179 15272179]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Schalk, I J.]]
[[Category: Schalk, I J.]]
[[Category: Tonb dependent receptor]]
[[Category: Tonb dependent receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:08:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:41:05 2008''

Revision as of 04:41, 28 July 2008

Template:STRUCTURE 1xkh

Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine

Template:ABSTRACT PUBMED 15733922

About this Structure

1XKH is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution., Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F, J Mol Biol. 2005 Mar 18;347(1):121-34. Epub 2005 Jan 21. PMID:15733922

Crystallization and preliminary X-ray analysis of the outer membrane pyoverdine receptor FpvA from Pseudomonas aeruginosa., Cobessi D, Celia H, Folschweiller N, Heymann M, Schalk I, Abdallah M, Pattus F, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1467-9. Epub 2004, Jul 21. PMID:15272179

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