3QQ2
Crystal Structure of the Beta Domain of the Bordetella Autotransporter Brka
3QQ2 の概要
| エントリーDOI | 10.2210/pdb3qq2/pdb |
| 分子名称 | BrkA autotransporter (1 entity in total) |
| 機能のキーワード | beta barrel, transmembrane, membrane protein-protein transport complex, membrane protein/protein transport |
| 由来する生物種 | Bordetella pertussis |
| 細胞内の位置 | BrkA autotransporter: Periplasm (By similarity). Serum resistance protein BrkA: Secreted. BrkA translocator: Cell outer membrane; Multi-pass membrane protein (Probable): Q45340 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 92965.00 |
| 構造登録者 | |
| 主引用文献 | Zhai, Y.,Zhang, K.,Huo, Y.,Zhu, Y.,Zhou, Q.,Lu, J.,Black, I.,Pang, X.,Roszak, A.W.,Zhang, X.,Isaacs, N.W.,Sun, F. Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the beta-domain pore Biochem.J., 435:577-587, 2011 Cited by PubMed Abstract: Whooping cough (pertussis) is a highly contagious acute respiratory illness of humans caused by the Gram-negative bacterial pathogen Bordetella pertussis. The AT (autotransporter) BrkA (Bordetella serum-resistance killing protein A) is an important B. pertussis virulence factor that confers serum resistance and mediates adherence. In the present study, we have solved the crystal structure of the BrkA β-domain at 3 Å (1 Å=0.1 nm) resolution. Special features are a hairpin-like structure formed by the external loop L4, which is observed fortuitously sitting inside the pore of the crystallographic adjacent β-domain, and a previously undiscovered hydrophobic cavity formed by patches on loop L4 and β-strands S5 and S6. This adopts a ubiquitous structure characteristic of all AT β-domains. Mutagenesis studies have demonstrated that the hairpin-like structure and hydrophobic cavity are crucial for BrkA passenger domain (virulence effector) translocation. This structure helps in understanding the molecular mechanism of AT assembly and secretion and provides a potential target for anti-pertussis drug design. PubMed: 21306302DOI: 10.1042/BJ20101548 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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