Structural highlights
Function
MOLB_HAEIN Part of the ABC transporter complex MolBCA involved in molybdate import (PubMed:22078568, PubMed:24722984). Responsible for the translocation of the substrate across the membrane (PubMed:24722984). Functions as a low-affinity molybdate transporter (PubMed:24722984).[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tirado-Lee L, Lee A, Rees DC, Pinkett HW. Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA. Structure. 2011 Nov 9;19(11):1701-10. PMID:22078568 doi:10.1016/j.str.2011.10.004
- ↑ Rice AJ, Harrison A, Alvarez FJ, Davidson AL, Pinkett HW. Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment. J Biol Chem. 2014 May 23;289(21):15005-13. PMID:24722984 doi:10.1074/jbc.M114.563783
- ↑ 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
