Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein.
Structure
; 25(9): 1455-1460.e2, 2017 09 05.
Article
em En
| MEDLINE
| ID: mdl-28877507
ABSTRACT
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 Å resolution. Two sets of six transmembrane α 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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Brassicaceae
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article