Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.4
Classification:METAL TRANSPORT
Release Date:2007-01-02
Deposition Date:2006-10-30
Revision Date:2008-05-01#2011-07-13
Molecular Weight:130201.05
Macromolecule Type:Protein
Residue Count:1180
Atom Site Count:8567
DOI:10.2210/pdb2nq2/pdb
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.
Resolution:2.4
Classification:METAL TRANSPORT
Release Date:2007-01-02
Deposition Date:2006-10-30
Revision Date:2008-05-01#2011-07-13
Molecular Weight:130201.05
Macromolecule Type:Protein
Residue Count:1180
Atom Site Count:8567
DOI:10.2210/pdb2nq2/pdb
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.
| Date made available | 2007 |
|---|---|
| Publisher | RCSB-PDB |