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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
42
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pubmed:dateCreated |
2003-10-13
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pubmed:abstractText |
Pasteurellosis caused by the Gram-negative pathogen Pasteurella haemolytica is a serious disease leading to death in cattle. To scavenge growth-limiting iron from the host, the pathogen utilizes the periplasmic ferric ion-binding protein A (PhFbpA) as a component of an ATP-binding cassette transport pathway. We report the 1.2-A structure of the iron-free (apo) form of PhFbpA, which is a member of the transferrin structural superfamily. The protein structure adopts a closed conformation, allowing us to reliably assign putative iron-coordinating residues. Based on our analysis, PhFbpA utilizes a unique constellation of binding site residues and anions to octahedrally coordinate an iron atom. A surprising finding in the structure is the presence of two formate anions on opposite sides of the iron-binding pocket. The formate ions tether the N- and C-terminal domains of the protein and stabilize the closed structure, also providing clues as to probable candidates for synergistic anions in the iron-loaded state. PhFbpA represents a new class of bacterial iron-binding proteins.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:DouganDouglas RDR,
pubmed-author:HosfieldDavid JDJ,
pubmed-author:KirbyShaneS,
pubmed-author:McReeDuncan EDE,
pubmed-author:ScheibeDanielD,
pubmed-author:SchryversAnthony BAB,
pubmed-author:ShouldiceStephen RSR,
pubmed-author:SkeneRobert JRJ,
pubmed-author:SnellGyorgyG,
pubmed-author:TariLeslie WLW,
pubmed-author:WilliamsPamela APA
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41093-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12882966-Bacterial Outer Membrane Proteins,
pubmed-meshheading:12882966-Bacterial Proteins,
pubmed-meshheading:12882966-Binding Sites,
pubmed-meshheading:12882966-Crystallography, X-Ray,
pubmed-meshheading:12882966-Escherichia coli,
pubmed-meshheading:12882966-Ions,
pubmed-meshheading:12882966-Iron,
pubmed-meshheading:12882966-Iron-Binding Proteins,
pubmed-meshheading:12882966-Mannheimia haemolytica,
pubmed-meshheading:12882966-Models, Molecular,
pubmed-meshheading:12882966-Periplasmic Binding Proteins,
pubmed-meshheading:12882966-Protein Binding,
pubmed-meshheading:12882966-Protein Conformation,
pubmed-meshheading:12882966-Protein Structure, Tertiary,
pubmed-meshheading:12882966-Transferrin
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pubmed:year |
2003
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pubmed:articleTitle |
Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins.
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pubmed:affiliation |
Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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