Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit.

ABSTRACT: ATP-binding cassette (ABC) transporters are membrane-bound molecular pumps that form one of the largest of all protein families. Several of them are central to phenomena of biomedical interest, including cystic fibrosis and resistance to chemotherapeutic drugs. ABC transporters share a common architecture comprising two hydrophilic nucleotide-binding domains (NBDs) and two hydrophobic transmembrane domains (TMDs) that form the substrate pathway across the membrane. The conformational changes in the NBDs induced by ATP hydrolysis and the means by which they are transmitted to the TMDs to effect substrate translocation remain largely unknown. We have performed a molecular dynamics simulation of HisP, the well studied NBD of the bacterial histidine permease, to identify hinges and switches of

SUBMITTER: Jones PM 

PROVIDER: S-EPMC130513 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature