7DJ1

Crystal structure of the G26C mutant of LeuT

7DJ1 の概要

• エントリーDOI: 10.2210/pdb7dj1/pdb
• 関連するPDBエントリー: 7DII 7DIX 7DJ2 7DJC
• 分子名称: Na(+):neurotransmitter symporter (Snf family), LEUCINE, SODIUM ION (3 entities in total)
• 機能のキーワード: neurotransmitter transporter, nss, slc6, 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: 115351.87

構造登録者

Fan, J.,Xiao, Y.,Sun, Z.,Zhou, X. (登録日: 2020-11-19, 公開日: 2021-04-07, 最終更新日: 2023-11-29)

主引用文献

Fan, J.,Xiao, Y.,Quick, M.,Yang, Y.,Sun, Z.,Javitch, J.A.,Zhou, X.
Crystal structures of LeuT reveal conformational dynamics in the outward-facing states.
J.Biol.Chem., 296:100609-100609, 2021

PubMed Abstract: The neurotransmitter:sodium symporter (NSS) homolog LeuT from Aquifex aeolicus has proven to be a valuable model for studying the transport mechanism of the NSS family. Crystal structures have captured LeuT in key conformations visited during the transport cycle, allowing for the construction of a nearly complete model of transport, with much of the conformational dynamics studied by computational simulations. Here, we report crystal structures of LeuT representing new intermediate conformations between the outward-facing open and occluded states. These structures, combined with binding and accessibility studies, reveal details of conformational dynamics that can follow substrate binding at the central substrate binding site (S1) of LeuT in outward-facing states, suggesting a potential competition for direction between the outward-open and outward-occluded states at this stage during substrate transport. Our structures further support an intimate interplay between the protonation state of Glu290 and binding of Na1 that may ultimately regulate the outward-open-to-occluded transition.

PubMed: 33811858
DOI: 10.1016/j.jbc.2021.100609

実験手法

X-RAY DIFFRACTION (3.528 Å)