Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex.

ABSTRACT: ATP-Binding Cassette transporters are ubiquitous membrane proteins that convert the energy from ATP-binding and hydrolysis into conformational changes of the transmembrane region to allow the translocation of substrates against their concentration gradient. Despite the large amount of structural and biochemical data available for this family, it is still not clear how the energy obtained from ATP hydrolysis in the ATPase domains is "transmitted" to the transmembrane domains. In this work, we focus our attention on the consequences of hydrolysis and inorganic phosphate exit in the maltose uptake system (MalFGK(2)E) from Escherichia coli. The prime goal is to identify and map the structural changes occurring during an ATP-hydrolytic cycle. For that, we use extensive molecular dynamics simula

SUBMITTER: Oliveira AS 

PROVIDER: S-EPMC3150292 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature