X-ray structure of the Yersinia pestis heme transporter HmuUV

Jae Sung Woo, Antra Zeltina, Birke A. Goetz, Kaspar P. Locher

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

HmuUV is a bacterial ATP-binding cassette (ABC) transporter that catalyzes heme uptake into the cytoplasm of the Gram-negative pathogen Yersinia pestis. We report the crystal structure of HmuUV at 3.0 Å resolution in a nucleotide-free state, which features a heme translocation pathway in an outward-facing conformation, poised to accept a heme from the cognate periplasmic binding protein HmuT. A new assay allowed us to determine in vitro rates of HmuUV-catalyzed heme transport into proteoliposomes and to establish the role of conserved residues in the translocation pathway of HmuUV and at the interface with HmuT. Differences in architecture relative to the related vitamin B 12 transporter BtuCD suggest an adaptation of HmuUV for its smaller substrate. Our study also suggests that type II ABC importers, which include bacterial iron-siderophore, heme and cobalamin transporters, have a coupling mechanism distinct from that of other ABC transporters.

Original languageEnglish
Pages (from-to)1310-1315
Number of pages6
JournalNature Structural and Molecular Biology
Volume19
Issue number12
DOIs
Publication statusPublished - 2012 Dec 1
Externally publishedYes

Fingerprint

Yersinia pestis
Heme
X-Rays
ATP-Binding Cassette Transporters
Vitamin B 12
Periplasmic Binding Proteins
Siderophores
Cytoplasm
Nucleotides
Iron
Adenosine Triphosphate

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

X-ray structure of the Yersinia pestis heme transporter HmuUV. / Woo, Jae Sung; Zeltina, Antra; Goetz, Birke A.; Locher, Kaspar P.

In: Nature Structural and Molecular Biology, Vol. 19, No. 12, 01.12.2012, p. 1310-1315.

Research output: Contribution to journalArticle

Woo, Jae Sung ; Zeltina, Antra ; Goetz, Birke A. ; Locher, Kaspar P. / X-ray structure of the Yersinia pestis heme transporter HmuUV. In: Nature Structural and Molecular Biology. 2012 ; Vol. 19, No. 12. pp. 1310-1315.
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