An inward-facing conformation of a putative metal-chelate-type ABC transporter
METADATA ONLY
Loading...
Author / Producer
Date
2007-01-19
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
METADATA ONLY
Data
Rights / License
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 B12 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.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
315 (5810)
Pages / Article No.
373 - 377
Publisher
Science
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
Organisational unit
03652 - Locher, Kaspar / Locher, Kaspar