3WX6
Crystal structure of Type Six Secretion System protein
3WX6 の概要
| エントリーDOI | 10.2210/pdb3wx6/pdb |
| 分子名称 | Uncharacterized protein (2 entities in total) |
| 機能のキーワード | hexameric assembly, hexameric ring, t6ss protein, unknown function |
| 由来する生物種 | Burkholderia pseudomallei K96243 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 38093.21 |
| 構造登録者 | |
| 主引用文献 | Lim, Y.T.,Jobichen, C.,Wong, J.,Limmathurotsakul, D.,Li, S.,Chen, Y.,Raida, M.,Srinivasan, N.,MacAry, P.A.,Sivaraman, J.,Gan, Y.H. Extended Loop Region of Hcp1 is Critical for the Assembly and Function of Type VI Secretion System in Burkholderia pseudomallei. Sci Rep, 5:8235-8235, 2015 Cited by PubMed Abstract: The Type VI Secretion System cluster 1 (T6SS1) is essential for the pathogenesis of Burkholderia pseudomallei, the causative agent of melioidosis, a disease endemic in the tropics. Inside host cells, B. pseudomallei escapes into the cytosol and through T6SS1, induces multinucleated giant cell (MNGC) formation that is thought to be important for bacterial cell to cell spread. The hemolysin-coregulated protein (Hcp) is both a T6SS substrate, as well as postulated to form part of the T6SS secretion tube. Our structural study reveals that Hcp1 forms hexameric rings similar to the other Hcp homologs but has an extended loop (Asp40-Arg56) that deviates significantly in position compared to other Hcp structures and may act as a key contact point between adjacent hexameric rings. When two residues within the loop were mutated, the mutant proteins were unable to stack as dodecamers, suggesting defective tube assembly. Moreover, infection with a bacterial mutant containing in situ substitution of these hcp1 residues abolishes Hcp1 secretion inside infected cells and MNGC formation. We further show that Hcp has the ability to preferentially bind to the surface of antigen-presenting cells, which may contribute to its immunogenicity in inducing high titers of antibodies seen in melioidosis patients. PubMed: 25648885DOI: 10.1038/srep08235 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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