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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2005-9-13
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pubmed:databankReference |
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pubmed:abstractText |
Pyochelin is a siderophore and virulence factor common to Burkholderia cepacia and several Pseudomonas strains. We describe at 2.0 A resolution the crystal structure of the pyochelin outer membrane receptor FptA bound to the iron-pyochelin isolated from Pseudomonas aeruginosa. One pyochelin molecule bound to iron is found in the protein structure, providing the first three-dimensional structure at the atomic level of this siderophore. The pyochelin molecule provides a tetra-dentate coordination of iron, while the remaining bi-dentate coordination is ensured by another molecule not specifically recognized by the protein. The overall structure of the pyochelin receptor is typical of the TonB-dependent transporter superfamily, which uses the proton motive force from the cytoplasmic membrane through the TonB-ExbB-ExbD energy transducing complex to transport ferric ions across the bacterial outer membrane: a transmembrane 22 beta-stranded barrel occluded by a N-terminal domain that contains a mixed four-stranded beta-sheet. The N-terminal TonB box is disordered in two crystal forms, and loop L8 is found to point towards the iron-pyochelin complex, suggesting that the receptor is in a transport-competent conformation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FPTA protein, Pseudomonas,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Iron Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Phenols,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Siderophores,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/pyochelin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
352
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
893-904
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16139844-Amino Acid Sequence,
pubmed-meshheading:16139844-Animals,
pubmed-meshheading:16139844-Bacterial Outer Membrane Proteins,
pubmed-meshheading:16139844-Binding Sites,
pubmed-meshheading:16139844-Crystallography, X-Ray,
pubmed-meshheading:16139844-Iron,
pubmed-meshheading:16139844-Iron Chelating Agents,
pubmed-meshheading:16139844-Models, Molecular,
pubmed-meshheading:16139844-Molecular Sequence Data,
pubmed-meshheading:16139844-Molecular Structure,
pubmed-meshheading:16139844-Phenols,
pubmed-meshheading:16139844-Protein Binding,
pubmed-meshheading:16139844-Protein Structure, Quaternary,
pubmed-meshheading:16139844-Protein Structure, Secondary,
pubmed-meshheading:16139844-Pseudomonas aeruginosa,
pubmed-meshheading:16139844-Receptors, Cell Surface,
pubmed-meshheading:16139844-Siderophores,
pubmed-meshheading:16139844-Thiazoles
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pubmed:year |
2005
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pubmed:articleTitle |
Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa.
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pubmed:affiliation |
Département Récepteurs et Protéines Membranaires, UMR7100 CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67412 Illkirch, France. cobessi@esbs.u.strasbg.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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