2A65

Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters

2A65 の概要

• エントリーDOI: 10.2210/pdb2a65/pdb
• 分子名称: Na(+):neurotransmitter symporter (Snf family), octyl beta-D-glucopyranoside, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: membrane protein, transport protein
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59751.89

構造登録者

Yamashita, A.,Singh, S.K.,Kawate, T.,Jin, Y.,Gouaux, E. (登録日: 2005-07-01, 公開日: 2005-08-02, 最終更新日: 2024-02-14)

主引用文献

Yamashita, A.,Singh, S.K.,Kawate, T.,Jin, Y.,Gouaux, E.
Crystal structure of a bacterial homologue of Na(+)/Cl(-)-dependent neurotransmitter transporters.
Nature, 437:215-223, 2005

PubMed Abstract: Na+/Cl--dependent transporters terminate synaptic transmission by using electrochemical gradients to drive the uptake of neurotransmitters, including the biogenic amines, from the synapse to the cytoplasm of neurons and glia. These transporters are the targets of therapeutic and illicit compounds, and their dysfunction has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane segments, with segments 1-5 related to 6-10 by a pseudo-two-fold axis in the membrane plane. Leucine and the sodium ions are bound within the protein core, halfway across the membrane bilayer, in an occluded site devoid of water. The leucine and ion binding sites are defined by partially unwound transmembrane helices, with main-chain atoms and helix dipoles having key roles in substrate and ion binding. The structure reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.

PubMed: 16041361
DOI: 10.1038/nature03978

実験手法

X-RAY DIFFRACTION (1.65 Å)