3QDC

Crystal structure of Natronomonas pharaonis sensory rhodopsin II in the active state

3QDC の概要

• エントリーDOI: 10.2210/pdb3qdc/pdb
• 分子名称: Sensory rhodopsin-2, RETINAL, octyl beta-D-glucopyranoside, ... (6 entities in total)
• 機能のキーワード: phototaxis, nphtrii, membrane, membrane protein
• 由来する生物種: Natronomonas pharaonis (Natronobacterium pharaonis)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P42196
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35445.80

構造登録者

Gushchin, I.,Reshetnyak, A.,Borshchevskiy, V.,Ishchenko, A.,Round, E.,Grudinin, S.,Engelhard, M.,Buldt, G.,Gordeliy, V. (登録日: 2011-01-18, 公開日: 2011-09-14, 最終更新日: 2024-02-21)

主引用文献

Gushchin, I.,Reshetnyak, A.,Borshchevskiy, V.,Ishchenko, A.,Round, E.,Grudinin, S.,Engelhard, M.,Buldt, G.,Gordeliy, V.
Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping.
J.Mol.Biol., 412:591-600, 2011

PubMed Abstract: The molecular mechanism of transmembrane signal transduction is still a pertinent question in cellular biology. Generally, a receptor can transfer an external signal via its cytoplasmic surface, as found for G-protein-coupled receptors such as rhodopsin, or via the membrane domain, such as that in sensory rhodopsin II (SRII) in complex with its transducer, HtrII. In the absence of HtrII, SRII functions as a proton pump. Here, we report on the crystal structure of the active state of uncomplexed SRII from Natronomonas pharaonis, NpSRII. The problem with a dramatic loss of diffraction quality upon loading of the active state was overcome by growing better crystals and by reducing the occupancy of the state. The conformational changes in the region comprising helices F and G are similar to those observed for the NpSRII-transducer complex but are much more pronounced. The meaning of these differences for the understanding of proton pumping and signal transduction by NpSRII is discussed.

PubMed: 21840321
DOI: 10.1016/j.jmb.2011.07.022

実験手法

X-RAY DIFFRACTION (2.5 Å)