2nq2
From Proteopedia
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An inward-facing conformation of a putative metal-chelate type ABC transporter.
Overview
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.
About this Structure
2NQ2 is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
An inward-facing conformation of a putative metal-chelate-type ABC transporter., Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC, Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7. PMID:17158291
Page seeded by OCA on Wed Nov 21 12:50:32 2007
