Conformational coupling of the nucleotide-binding and the transmembrane domains in ABC transporters.

ABSTRACT: Basic architecture of ABC transporters includes two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). Although the transport process takes place in the TMDs, which provide the substrate translocation pathway across the cell membrane and control its accessibility between the two sides of the membrane, the energy required for the process is provided by conformational changes induced in the NBDs by binding and hydrolysis of ATP. Nucleotide-dependent conformational changes in the NBDs, therefore, need to be coupled to structural changes in the TMDs. Using molecular dynamics simulations, we have investigated the structural elements involved in the conformational coupling between the NBDs and the TMDs in the Escherichia coli maltose transporter, an ABC importer for which an

SUBMITTER: Wen PC 

PROVIDER: S-EPMC3145290 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature