Energy coupling mechanisms of MFS transporters.
Protein Sci
; 24(10): 1560-79, 2015 Oct.
Article
em En
| MEDLINE
| ID: mdl-26234418
ABSTRACT
Major facilitator superfamily (MFS) is a large class of secondary active transporters widely expressed across all life kingdoms. Although a common 12-transmembrane helix-bundle architecture is found in most MFS crystal structures available, a common mechanism of energy coupling remains to be elucidated. Here, we discuss several models for energy-coupling in the transport process of the transporters, largely based on currently available structures and the results of their biochemical analyses. Special attention is paid to the interaction between protonation and the negative-inside membrane potential. Also, functional roles of the conserved sequence motifs are discussed in the context of the 3D structures. We anticipate that in the near future, a unified picture of the functions of MFS transporters will emerge from the insights gained from studies of the common architectures and conserved motifs.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Membrana Transportadoras
/
Metabolismo Energético
/
Modelos Biológicos
Idioma:
En
Revista:
Protein Sci
Ano de publicação:
2015
Tipo de documento:
Article