Structural highlights
Publication Abstract from PubMed
The multidrug and toxic compound extrusion (MATE) family of proteins consists of transporters responsible for multidrug resistance in prokaryotes. In plants, a number of MATE proteins were identified by recent genomic and functional studies, which imply that the proteins have substrate-specific transport functions instead of multidrug extrusion. The three-dimensional structure of eukaryotic MATE proteins, including those of plants, has not been reported, preventing a better understanding of the molecular mechanism of these proteins. Here, we describe the crystal structure of a MATE protein from the plant Camelina sativa at 2.9 A resolution. Two sets of six transmembrane alpha helices, assembled pseudo-symmetrically, possess a negatively charged internal pocket with an outward-facing shape. The crystal structure provides insight into the diversity of plant MATE proteins and their substrate recognition and transport through the membrane.
Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein.,Tanaka Y, Iwaki S, Tsukazaki T Structure. 2017 Sep 5;25(9):1455-1460.e2. doi: 10.1016/j.str.2017.07.009. PMID:28877507[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tanaka Y, Iwaki S, Tsukazaki T. Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein. Structure. 2017 Sep 5;25(9):1455-1460.e2. doi: 10.1016/j.str.2017.07.009. PMID:28877507 doi:http://dx.doi.org/10.1016/j.str.2017.07.009
