3BK6
Crystal structure of a core domain of stomatin from Pyrococcus horikoshii
3BK6 の概要
エントリーDOI | 10.2210/pdb3bk6/pdb |
分子名称 | PH stomatin (1 entity in total) |
機能のキーワード | stomatin, archaea, pyrococcus horikoshii, trimer, coiled-coil, flotillin, spfh, membrane fusion, trafficking, transmembrane, membrane protein |
由来する生物種 | Pyrococcus horikoshii |
細胞内の位置 | Membrane; Single-pass membrane protein (Potential): O59180 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 63892.19 |
構造登録者 | |
主引用文献 | Yokoyama, H.,Fujii, S.,Matsui, I. Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold J.Mol.Biol., 376:868-878, 2008 Cited by PubMed Abstract: Stomatin is a major integral membrane protein of human erythrocytes, the absence of which is associated with a form of hemolytic anemia known as hereditary stomatocytosis. However, the function of stomatin is not fully understood. An open reading frame, PH1511, from the hyperthermophilic archaeon Pyrococcus horikoshii encodes p-stomatin, a prokaryotic stomatin. Here, we report the first crystal structure of a stomatin ortholog, the core domain of the p-stomatin PH1511p (residues 56-234 of PH1511p, designated as PhSto(CD)). PhSto(CD) forms a novel homotrimeric structure. Three alpha/beta domains form a triangle of about 50 A on each side, and three alpha-helical segments of about 60 A in length extend from the apexes of the triangle. The alpha/beta domain of PhSto(CD) is partly similar in structure to the band-7 domain of mouse flotillin-2. While the alpha/beta domain is relatively rigid, the alpha-helical segment shows conformational flexibility, adapting to the neighboring environment. One alpha-helical segment forms an anti-parallel coiled coil with another alpha-helical segment from a symmetry-related molecule. The alpha-helical segment shows a heptad repeat pattern, and mainly hydrophobic residues form a coiled-coil interface. According to chemical cross-linking experiments, PhSto(CD) would be able to assemble into an oligomeric form. The coiled-coil fold observed in the crystal probably contributes to self-association. PubMed: 18182167DOI: 10.1016/j.jmb.2007.12.024 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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