1Y9T
Crystal structure of a type III secretion system protein complexed with the lipid, 1-monohexanoyl-2-hydroxy-sn-glycero-3-phosphate
1Y9T の概要
エントリーDOI | 10.2210/pdb1y9t/pdb |
関連するPDBエントリー | 1Y9L |
分子名称 | Lipoprotein mxiM, ACETATE ION, (2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL HEXANOATE, ... (4 entities in total) |
機能のキーワード | mixed alpha/beta, cracked b-barrel fold, lipid binding protein |
由来する生物種 | Shigella flexneri |
細胞内の位置 | Cell outer membrane; Lipid-anchor (Probable): P0A1X2 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 13233.15 |
構造登録者 | |
主引用文献 | Lario, P.I.,Pfuetzner, R.A.,Frey, E.A.,Creagh, L.,Haynes, C.,Maurelli, A.T.,Strynadka, N.C. Structure and biochemical analysis of a secretin pilot protein. Embo J., 24:1111-1121, 2005 Cited by PubMed Abstract: The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion apparatus, the assembly of the TTSS complex requires the preceding formation of its integral outer membrane secretin ring component. We have determined at 1.5 A the structure of MxiM28-142, the Shigella pilot protein that is essential for the assembly and membrane association of the Shigella secretin, MxiD. This represents the first atomic structure of a secretin pilot protein from the several bacterial secretion systems containing an orthologous secretin component. A deep hydrophobic cavity is observed in the novel 'cracked barrel' structure of MxiM, providing a specific binding domain for the acyl chains of bacterial lipids, a proposal that is supported by our various lipid/MxiM complex structures. Isothermal titration analysis shows that the C-terminal domain of the secretin, MxiD525-570, hinders lipid binding to MxiM. PubMed: 15775974DOI: 10.1038/sj.emboj.7600610 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.87 Å) |
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