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Nat Commun ; 7: 13411, 2016 11 10.
Article in English | MEDLINE | ID: mdl-27830695

ABSTRACT

Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal structures of Burkholderia cenocepacia haem importer BhuUV complexed with the periplasmic haem-binding protein BhuT and in the absence of BhuT. The transmembrane helices of these structures show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of the type II importer. Structural comparison with the outward-facing conformation reported for the haem importer ortholog HmuUV from Yersenia pestis gives mechanistic insights into conformational transitions and haem secretion during the haem transport cycle.


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Bacterial Proteins/metabolism , Heme/metabolism , Periplasm/metabolism , ATP-Binding Cassette Transporters/chemistry , ATP-Binding Cassette Transporters/genetics , Amino Acid Sequence , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Biological Transport , Burkholderia cenocepacia/genetics , Burkholderia cenocepacia/metabolism , Carrier Proteins/chemistry , Carrier Proteins/genetics , Carrier Proteins/metabolism , Crystallography, X-Ray , Heme/chemistry , Heme-Binding Proteins , Hemeproteins/chemistry , Hemeproteins/genetics , Hemeproteins/metabolism , Models, Molecular , Protein Conformation , Sequence Homology, Amino Acid
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