An inward-facing conformation of a putative metal-chelate-type ABC transporter

H. W. Pinkett, A. T. Lee, P. Lum, K. P. Locher, D. C. Rees*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

227 Scopus citations

Abstract

The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B 12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.

Original languageEnglish (US)
Pages (from-to)373-377
Number of pages5
JournalScience
Volume315
Issue number5810
DOIs
StatePublished - Jan 19 2007

ASJC Scopus subject areas

  • General

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