2nq2
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| , resolution 2.400Å | |||||||
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| Gene: | HI_1471 (Haemophilus influenzae), HI_1470 (Haemophilus influenzae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
An inward-facing conformation of a putative metal-chelate type ABC transporter.
OverviewOverview
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 StructureAbout this Structure
2NQ2 is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.
ReferenceReference
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
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