2NQ2

An inward-facing conformation of a putative metal-chelate type ABC transporter.

Summary for 2NQ2

• Entry DOI: 10.2210/pdb2nq2/pdb
• Descriptor: Hypothetical ABC transporter permease protein HI1471, Hypothetical ABC transporter ATP-binding protein HI1470 (3 entities in total)
• Functional Keywords: putative iron chelatin abc transporter, atp-binding protein, nucleotide binding domain, transmembrane domain, metal transport
• Biological source: Haemophilus influenzae; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein (Potential): Q57130
• Total number of polymer chains: 4
• Total formula weight: 130201.06

Authors

Pinkett, H.P.,Lee, A.T.,Lum, P.,Locher, K.P.,Rees, D.C. (deposition date: 2006-10-30, release date: 2007-01-02, Last modification date: 2023-12-27)

Primary citation

Pinkett, H.W.,Lee, A.T.,Lum, P.,Locher, K.P.,Rees, D.C.
An inward-facing conformation of a putative metal-chelate-type ABC transporter.
Science, 315:373-377, 2007

PubMed 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.

PubMed: 17158291
DOI: 10.1126/science.1133488

Experimental method

X-RAY DIFFRACTION (2.4 Å)