The Amino Terminus of LeuT Changes Conformation in an Environment Sensitive Manner.

ABSTRACT: Neurotransmitter:sodium symporters are highly expressed in the human brain and catalyze the uptake of substrate through the plasma membrane by using the electrochemical gradient of sodium as the energy source. The bacterial homolog LeuT, a small amino acid transporter isolated from the bacteria Aquifex aeolicus, is the founding member of the family and has been crystallized in three conformations. The N-terminus is structurally well defined and strongly interacts with the transporter core in the outward-facing conformations. However, it could not be resolved in the inward-facing conformation, which indicates enhanced mobility. Here we investigate conformations and dynamics of the N-terminus, by combining molecular dynamics simulations with experimental verification using distance measureme

SUBMITTER: Khan JA 

PROVIDER: S-EPMC7260283 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature