4J3O
Crystal structure of the FimD usher traversed by the pilus tip complex assembly composed of FimC:FimF:FimG:FimH
4J3O の概要
| エントリーDOI | 10.2210/pdb4j3o/pdb |
| 分子名称 | Protein FimG, Protein FimH, Chaperone protein FimC, ... (5 entities in total) |
| 機能のキーワード | beta barrel, immunglobuline-like fold, type 1 pilus assembly, pilus subunit translocation, adhesion, d-mannose-binding, bacterial outer membrane, cell adhesion-chaperone-membrane protein complex, cell adhesion/chaperone/membrane protein |
| 由来する生物種 | Escherichia coli 詳細 |
| 細胞内の位置 | Fimbrium: P08190 P08191 P08189 Periplasm: P31697 Cell outer membrane; Multi-pass membrane protein (By similarity): P30130 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 176345.78 |
| 構造登録者 | |
| 主引用文献 | Geibel, S.,Procko, E.,Hultgren, S.J.,Baker, D.,Waksman, G. Structural and energetic basis of folded-protein transport by the FimD usher. Nature, 496:243-246, 2013 Cited by PubMed Abstract: Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion. The recent determination of the crystal structure of an initiation complex provided insight into the initiation step of pilus biogenesis resulting in pore activation, but very little is known about the elongation steps that follow. Here, to address this question, we determine the structure of an elongation complex in which the tip complex assembly composed of FimC, FimF, FimG and FimH passes through FimD. This structure demonstrates the conformational changes required to prevent backsliding of the nascent pilus through the FimD pore and also reveals unexpected properties of the usher pore. We show that the circular binding interface between the pore lumen and the folded substrate participates in transport by defining a low-energy pathway along which the nascent pilus polymer is guided during secretion. PubMed: 23579681DOI: 10.1038/nature12007 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.8 Å) |
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