4FBZ

Crystal structure of deltarhodopsin from Haloterrigena thermotolerans

4FBZ の概要

• エントリーDOI: 10.2210/pdb4fbz/pdb
• 関連するPDBエントリー: 1iw6
• 分子名称: deltarhodopsin, RETINAL, BACTERIORUBERIN, ... (8 entities in total)
• 機能のキーワード: 7 transmembrane helices, light-driven proton pump, cell membrane, membrane protein
• 由来する生物種: Haloterrigena thermotolerans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29158.25

構造登録者

Kouyama, T. (登録日: 2012-05-23, 公開日: 2013-05-15, 最終更新日: 2024-10-30)

主引用文献

Zhang, J.,Mizuno, K.,Murata, Y.,Koide, H.,Murakami, M.,Ihara, K.,Kouyama, T.
Crystal structure of deltarhodopsin-3 from Haloterrigena thermotolerans
Proteins, 81:1585-1592, 2013

PubMed Abstract: Deltarhodopsin, a new member of the microbial rhodopsin family, functions as a light-driven proton pump. Here, we report the three-dimensional structure of deltarhodopsin (dR3) from Haloterrigena thermotolerans at 2.7 Å resolution. A crystal belonging to space group R32 (a, b = 111.71 Å, c = 198.25 Å) was obtained by the membrane fusion method. In this crystal, dR3 forms a trimeric structure as observed for bacteriorhodopsin (bR). Structural comparison of dR with bR showed that the inner part (the proton release and uptake pathways) is highly conserved. Meanwhile, residues in the protein-protein contact region are largely altered so that the diameter of the trimeric structure at the cytoplasmic side is noticeably larger in dR3. Unlike bR, dR3 possesses a helical segment at the C-terminal region that fills the space between the AB and EF loops. A significant difference is also seen in the FG loop, which is one residue longer in dR3. Another peculiar property of dR3 is a highly crowded distribution of positively charged residues on the cytoplasmic surface, which may be relevant to a specific interaction with some cytoplasmic component.

PubMed: 23625688
DOI: 10.1002/prot.24316

実験手法

X-RAY DIFFRACTION (2.7 Å)