4FTF
Structure of the Type II secretion system pilotin AspS from Vibrio cholerae
4FTF の概要
| エントリーDOI | 10.2210/pdb4ftf/pdb |
| 分子名称 | Alternate secretin pathway subunit S (VC395_1821, VC1703), ZINC ION, ACETATE ION, ... (4 entities in total) |
| 機能のキーワード | pilotin, lipoprotein, secretin, protein secretion, pfamb pb000779, secretin binding, outer membrane, protein transport |
| 由来する生物種 | Vibrio cholerae |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12633.36 |
| 構造登録者 | |
| 主引用文献 | Dunstan, R.A.,Heinz, E.,Wijeyewickrema, L.C.,Pike, R.N.,Purcell, A.W.,Evans, T.J.,Praszkier, J.,Robins-Browne, R.M.,Strugnell, R.A.,Korotkov, K.V.,Lithgow, T. Assembly of the Type II Secretion System such as Found in Vibrio cholerae Depends on the Novel Pilotin AspS. Plos Pathog., 9:e1003117-e1003117, 2013 Cited by PubMed Abstract: The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS. PubMed: 23326233DOI: 10.1371/journal.ppat.1003117 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.48 Å) |
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