8TQE の概要
エントリーDOI | 10.2210/pdb8tqe/pdb |
EMDBエントリー | 41503 |
分子名称 | XptA2 (1 entity in total) |
機能のキーワード | tca, insecticide, translocase, toxin |
由来する生物種 | Xenorhabdus nematophila |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 1421960.94 |
構造登録者 | |
主引用文献 | Martin, C.L.,Chester, D.W.,Radka, C.D.,Pan, L.,Yang, Z.,Hart, R.C.,Binshtein, E.M.,Wang, Z.,Nagy, L.,DeLucas, L.J.,Aller, S.G. Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains. Int J Mol Sci, 24:-, 2023 Cited by PubMed Abstract: The Toxin Complex (Tc) superfamily consists of toxin translocases that contribute to the targeting, delivery, and cytotoxicity of certain pathogenic Gram-negative bacteria. Membrane receptor targeting is driven by the A-subunit (TcA), which comprises IgG-like receptor binding domains (RBDs) at the surface. To better understand XptA2, an insect specific TcA secreted by the symbiont from the intestine of entomopathogenic nematodes, we determined structures by X-ray crystallography and cryo-EM. Contrary to a previous report, XptA2 is pentameric. RBD-B exhibits an indentation from crystal packing that indicates loose association with the shell and a hotspot for possible receptor binding or a trigger for conformational dynamics. A two-fragment XptA2 lacking an intact linker achieved the folded pre-pore state like wild type (wt), revealing no requirement of the linker for protein folding. The linker is disordered in all structures, and we propose it plays a role in dynamics downstream of the initial pre-pore state. PubMed: 37686027DOI: 10.3390/ijms241713221 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
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