1Z21
Crystal structure of the core domain of Yersinia pestis virulence factor YopR
1Z21 の概要
エントリーDOI | 10.2210/pdb1z21/pdb |
分子名称 | Yop proteins translocation protein H (2 entities in total) |
機能のキーワード | yersinia pestis, plague, type iii secretion, yopr, yop, cell invasion |
由来する生物種 | Yersinia pestis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 12606.38 |
構造登録者 | Schubot, F.D.,Cherry, S.,Tropea, J.E.,Austin, B.P.,Waugh, D.S. (登録日: 2005-03-07, 公開日: 2005-06-07, 最終更新日: 2024-02-14) |
主引用文献 | Schubot, F.D.,Cherry, S.,Austin, B.P.,Tropea, J.E.,Waugh, D.S. Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR. Protein Sci., 14:1679-1683, 2005 Cited by PubMed Abstract: Yersinia pestis, the causative agent of the plague, employs a type III secretion system (T3SS) to secrete and translocate virulence factors into to the cytoplasm of mammalian host cells. One of the secreted virulence factors is YopR. Little is known about the function of YopR other than that it is secreted into the extracellular milieu during the early stages of infection and that it contributes to virulence. Hoping to gain some insight into the function of YopR, we determined the crystal structure of its protease-resistant core domain, which consists of residues 38-149 out of 165 amino acids. The core domain is composed of five alpha-helices that display unexpected structural similarity with one domain of YopN, a central regulator of type III secretion in Y. pestis. This finding raises the possibility that YopR may play a role in the regulation of type III secretion. PubMed: 15930010DOI: 10.1110/ps.051446405 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.499 Å) |
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