Crystal structure of bacterial haem importer complex in the inward-facing conformation

Youichi Naoe, Nozomi Nakamura, Akihiro Doi, Mia Sawabe, Hiro Nakamura, Yoshitsugu Shiro and Hiroshi Sugimoto ()
Additional contact information
Youichi Naoe: Biometal Science Laboratory
Nozomi Nakamura: Biometal Science Laboratory
Akihiro Doi: Biometal Science Laboratory
Mia Sawabe: University of Hyogo
Hiro Nakamura: Biometal Science Laboratory
Yoshitsugu Shiro: Biometal Science Laboratory
Hiroshi Sugimoto: Biometal Science Laboratory

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: 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.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms13411 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13411

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms13411

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().