3F3C

Crystal structure of LeuT bound to 4-Fluoro-L-Phenylalanine and sodium

3F3C の概要

• エントリーDOI: 10.2210/pdb3f3c/pdb
• 関連するPDBエントリー: 2A65 2QEI 3F3A 3F3D 3F3E 3F48 3F4I 3F4J
• 分子名称: Transporter, 4-FLUORO-L-PHENYLALANINE, octyl beta-D-glucopyranoside, ... (5 entities in total)
• 機能のキーワード: slc6, nss, transmembrane, sodium-coupled, transporter, symport, transport, 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: 59768.44

構造登録者

Singh, S.K.,Piscitelli, C.L.,Yamashita, A.,Gouaux, E. (登録日: 2008-10-30, 公開日: 2008-12-23, 最終更新日: 2023-09-06)

主引用文献

Singh, S.K.,Piscitelli, C.L.,Yamashita, A.,Gouaux, E.
A competitive inhibitor traps LeuT in an open-to-out conformation.
Science, 322:1655-1661, 2008

PubMed Abstract: Secondary transporters are workhorses of cellular membranes, catalyzing the movement of small molecules and ions across the bilayer and coupling substrate passage to ion gradients. However, the conformational changes that accompany substrate transport, the mechanism by which a substrate moves through the transporter, and principles of competitive inhibition remain unclear. We used crystallographic and functional studies on the leucine transporter (LeuT), a model for neurotransmitter sodium symporters, to show that various amino acid substrates induce the same occluded conformational state and that a competitive inhibitor, tryptophan (Trp), traps LeuT in an open-to-out conformation. In the Trp complex, the extracellular gate residues arginine 30 and aspartic acid 404 define a second weak binding site for substrates or inhibitors as they permeate from the extracellular solution to the primary substrate site, which demonstrates how residues that participate in gating also mediate permeation.

PubMed: 19074341
DOI: 10.1126/science.1166777

実験手法

X-RAY DIFFRACTION (2.1 Å)