3WWV

C-terminal domain of stomatin operon partner protein 1510-C from Pyrococcus horikoshii

3WWV の概要

• エントリーDOI: 10.2210/pdb3wwv/pdb
• 関連するPDBエントリー: 2DEO 2EXD 3BK6 3BPP 3VIV 3WG5
• 分子名称: Stomatin operon partner protein, SODIUM ION (3 entities in total)
• 機能のキーワード: beta barrel, ob fold, unknown function, membrane protein stomatin
• 由来する生物種: Pyrococcus horikoshii OT3
• 細胞内の位置: Membrane ; Multi-pass membrane protein : O59179
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9208.72

構造登録者

Yokoyama, H.,Matsui, I. (登録日: 2014-06-30, 公開日: 2014-10-01, 最終更新日: 2023-11-08)

主引用文献

Yokoyama, H.,Matsui, I.
Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly
FEBS Open Bio, 4:804-812, 2014

PubMed Abstract: Stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins are found in the lipid raft microdomains of various cellular membranes. Stomatin/STOPP (stomatin operon partner protein) gene pairs are present in both archaeal and bacterial species, and their protein products may be involved in the quality control of membrane proteins. In the present study, the crystal structure of the C-terminal soluble domain of STOPP PH1510 (1510-C) from the hyperthermophilic archaeon Pyrococcus horikoshii was determined at 2.4 Å resolution. The structure of 1510-C had a compact five-stranded β-barrel fold known as an oligosaccharide/oligonucleotide-binding fold (OB-fold). According to crystal packing, 1510-C could assemble into multimers based on a dimer as a basic unit. 1510-C also formed a large cylinder-like structure composed of 24 subunits or a large triangular prism-like structure composed of 12 subunits. These results indicate that 1510-C functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin.

PubMed: 25349784
DOI: 10.1016/j.fob.2014.09.002

実験手法

X-RAY DIFFRACTION (2.4 Å)