Structural highlights
Function
[Y1471_HAEIN] Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7. PMID:17158291
