Bacterial Leucine Transporter

Bacterial Leucine Transporter
Molecular dynamics simulation of LeuT generated using GROMACS
Identifiers
SymbolLeuT
PDB3F3E
RefSeqNC_000918.1. NP_214423.1. NC_000918.1.
UniProtO67854
Search for
StructuresSwiss-model
DomainsInterPro

Bacterial Leucine Transporter (LeuT) is a bundled twelve alpha helix protein which belongs to the family of transporters that shuttle amino acids in and out of bacterial cells. Specialized in small hydrophobic amino acids such as leucine and alanine, this transporter is powered by the gradient of sodium ions that is normally maintained by healthy cells across their membranes. LeuT acts as a symporter, which means that it links the passage of a sodium ion across the cell membrane with the transport of the amino acid in the same direction. It was first crystallized to understand the inner molecular mechanisms of antidepressant's work since it has a close resemblance with the human neurotransmitter transporters (more difficult to crystallize) that these drugs block, thus inhibiting the reuptake of chemical messengers across the cell membrane of nerve axons and glial cells.[1][2]

  1. ^ Zhou Z, Zhen J, Karpowich NK, Goetz RM, Law CJ, Reith ME, Wang DN (September 2007). "LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake". Science. 317 (5843). New York, N.Y.: 1390–1393. Bibcode:2007Sci...317.1390Z. doi:10.1126/science.1147614. PMC 3711652. PMID 17690258.
  2. ^ Singh SK, Yamashita A, Gouaux E (August 2007). "Antidepressant binding site in a bacterial homologue of neurotransmitter transporters". Nature. 448 (7156): 952–956. Bibcode:2007Natur.448..952S. doi:10.1038/nature06038. PMID 17687333. S2CID 4315958.

© MMXXIII Rich X Search. We shall prevail. All rights reserved. Rich X Search