2M3G

Structure of Anabaena Sensory Rhodopsin Determined by Solid State NMR Spectroscopy

2M3G の概要

• エントリーDOI: 10.2210/pdb2m3g/pdb
• 分子名称: Anabaena Sensory Rhodopsin, RETINAL (2 entities in total)
• 機能のキーワード: solid state nmr, anabaena sensory rhodopsin, mas nmr, trimers, membrane protein
• 由来する生物種: Nostoc sp. PCC 7120 (Cyanobacteria)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 82587.81

構造登録者

Wang, S.,Munro, R.A.,Shi, L.,Kawamura, I.,Okitsu, T.,Wada, A.,Kim, S.,Jung, K.,Brown, L.S.,Ladizhansky, V. (登録日: 2013-01-17, 公開日: 2013-08-21, 最終更新日: 2024-10-16)

主引用文献

Wang, S.,Munro, R.A.,Shi, L.,Kawamura, I.,Okitsu, T.,Wada, A.,Kim, S.Y.,Jung, K.H.,Brown, L.S.,Ladizhansky, V.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Nat.Methods, 10:1007-1012, 2013

PubMed Abstract: Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning solid-state NMR spectroscopy can be used to determine structures of membrane proteins reconstituted in synthetic lipids, an environment similar to the natural membrane. We combined a large number of experimentally determined interatomic distances and local torsional restraints to solve the structure of an oligomeric membrane protein of common seven-helical fold, Anabaena sensory rhodopsin (ASR). We determined the atomic resolution detail of the oligomerization interface of the ASR trimer, and the arrangement of helices, side chains and the retinal cofactor in the monomer.

PubMed: 24013819
DOI: 10.1038/nmeth.2635

実験手法

SOLID-STATE NMR