2J2Z

X-Ray Structure of the Chaperone PapD in complex with the Pilus terminator subunit PapH at 2.3 Angstrom resolution

2J2Z の概要

• エントリーDOI: 10.2210/pdb2j2z/pdb
• 関連するPDBエントリー: 1N0L 1PDK 1QPP 1QPX 3DPA
• 分子名称: CHAPERONE PROTEIN PAPD, PAP FIMBRIAL MINOR PILIN PROTEIN, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: chaperone/surface active protein, periplasmic, pilus termination, immunoglobulin domain, paph, papd, fimbria, chaperone, p5 pocket, chaperone- surface active protein complex, chaperone-surface active protein complex
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Periplasm: P15319; Secreted: P07111
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45003.23

構造登録者

Verger, D.,Miller, E.,Remaut, H.,Waksman, G.,Hultgren, S. (登録日: 2006-08-17, 公開日: 2006-11-08, 最終更新日: 2024-11-06)

主引用文献

Verger, D.,Miller, E.,Remaut, H.,Waksman, G.,Hultgren, S.
Molecular Mechanism of P Pilus Termination in Uropathogenic Escherichia Coli.
Embo Rep., 7:1228-, 2006

PubMed Abstract: P pili are important adhesive fibres that are assembled by the conserved chaperone-usher pathway. During pilus assembly, the subunits are incorporated into the growing fibre by the donor-strand exchange mechanism, whereby the beta-strand of the chaperone, which complements the incomplete immunoglobulin fold of each subunit, is displaced by the amino-terminal extension of an incoming subunit in a zip-in-zip-out exchange process that is initiated at the P5 pocket, an exposed hydrophobic pocket in the groove of the subunit. In vivo, termination of P pilus growth requires a specialized subunit, PapH. Here, we show that PapH is incorporated at the base of the growing pilus, where it is unable to undergo donor-strand exchange. This inability is not due to a stronger PapD-PapH interaction, but to a lack of a P5 initiator pocket in the PapH structure, suggesting that PapH terminates pilus growth because it is lacking the initiation point by which donor-strand exchange proceeds.

PubMed: 17082819
DOI: 10.1038/SJ.EMBOR.7400833

実験手法

X-RAY DIFFRACTION (2.3 Å)