3USO

Crystal structure of LeuT bound to L-selenomethionine in space group P21212 from lipid bicelles

3USO の概要

• エントリーDOI: 10.2210/pdb3uso/pdb
• 関連するPDBエントリー: 3USG 3USI 3USJ 3USK 3USL 3USM 3USP
• 分子名称: Transporter, SODIUM ION, SELENOMETHIONINE (3 entities in total)
• 機能のキーワード: leucine transporter, transport protein
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116639.05

構造登録者

Wang, H.,Elferich, J.,Gouaux, E. (登録日: 2011-11-23, 公開日: 2012-01-11, 最終更新日: 2023-12-06)

主引用文献

Wang, H.,Elferich, J.,Gouaux, E.
Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context.
Nat.Struct.Mol.Biol., 19:212-219, 2012

PubMed Abstract: Neurotransmitter sodium symporters (NSSs) catalyze the uptake of neurotransmitters into cells, terminating neurotransmission at chemical synapses. Consistent with the role of NSSs in the central nervous system, they are implicated in multiple diseases and disorders. LeuT, from Aquifex aeolicus, is a prokaryotic ortholog of the NSS family and has contributed to our understanding of the structure, mechanism and pharmacology of NSSs. At present, however, the functional state of LeuT in crystals grown in the presence of n-octyl-β-D-glucopyranoside (β-OG) and the number of substrate binding sites are controversial issues. Here we present crystal structures of LeuT grown in DMPC-CHAPSO bicelles and demonstrate that the conformations of LeuT-substrate complexes in lipid bicelles and in β-OG detergent micelles are nearly identical. Furthermore, using crystals grown in bicelles and the substrate leucine or the substrate analog selenomethionine, we find only a single substrate molecule in the primary binding site.

PubMed: 22245965
DOI: 10.1038/nsmb.2215

実験手法

X-RAY DIFFRACTION (4.5 Å)