3BK6
Crystal structure of a core domain of stomatin from Pyrococcus horikoshii
Summary for 3BK6
| Entry DOI | 10.2210/pdb3bk6/pdb |
| Descriptor | PH stomatin (1 entity in total) |
| Functional Keywords | stomatin, archaea, pyrococcus horikoshii, trimer, coiled-coil, flotillin, spfh, membrane fusion, trafficking, transmembrane, membrane protein |
| Biological source | Pyrococcus horikoshii |
| Cellular location | Membrane; Single-pass membrane protein (Potential): O59180 |
| Total number of polymer chains | 3 |
| Total formula weight | 63892.19 |
| Authors | Yokoyama, H.,Fujii, S.,Matsui, I. (deposition date: 2007-12-05, release date: 2008-02-19, Last modification date: 2024-03-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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