Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold |
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Authors: | Yokoyama Hideshi Fujii Satoshi Matsui Ikuo |
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Institution: | 1 School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan 2 Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan |
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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 PhStoCD). PhStoCD forms a novel homotrimeric structure. Three α/β domains form a triangle of about 50 Å on each side, and three α-helical segments of about 60 Å in length extend from the apexes of the triangle. The α/β domain of PhStoCD is partly similar in structure to the band-7 domain of mouse flotillin-2. While the α/β domain is relatively rigid, the α-helical segment shows conformational flexibility, adapting to the neighboring environment. One α-helical segment forms an anti-parallel coiled coil with another α-helical segment from a symmetry-related molecule. The α-helical segment shows a heptad repeat pattern, and mainly hydrophobic residues form a coiled-coil interface. According to chemical cross-linking experiments, PhStoCD would be able to assemble into an oligomeric form. The coiled-coil fold observed in the crystal probably contributes to self-association. |
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Keywords: | PhStoCD residues 56-234 of PH1511p ASIC acid-sensing ion channel stopp stomatin operon partner protein 1510-N residues 16-236 of PH1510p PDB Protein Data Bank MAD multiwavelength anomalous dispersion SeMet selenomethionine BSA buried surface area MPD 2-methyl-2 4-pentanediol |
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