1DAB

The Structure of Bordetella Pertussis Virulence Factor P.69 Pertactin

1DAB の概要

• エントリーDOI: 10.2210/pdb1dab/pdb
• 分子名称: P.69 PERTACTIN (2 entities in total)
• 機能のキーワード: pertussis beta helix, cell adhesion
• 由来する生物種: Bordetella pertussis
• 細胞内の位置: Pertactin autotransporter: Periplasm . Outer membrane protein P. Pertactin translocator: Cell outer membrane ; Multi-pass membrane protein : P14283
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54627.90

構造登録者

Emsley, P.,Charles, I.G.,Fairweather, N.F.,Isaacs, N.W. (登録日: 1999-10-31, 公開日: 1999-12-15, 最終更新日: 2024-02-07)

主引用文献

Emsley, P.,Charles, I.G.,Fairweather, N.F.,Isaacs, N.W.
Structure of Bordetella pertussis virulence factor P.69 pertactin.
Nature, 381:90-92, 1996

PubMed Abstract: A new generation of whooping-cough vaccines contain P.69 pertactin, a surface-exposed domain of an outer membrane protein expressed by the virulent bacterium Bordetella pertussis. This protein is a virulence factor that mediates adhesion to target mammalian cells, a reaction that is in part mediated by an RGD sequence. The X-ray crystal structure of P.69 pertactin has been determined to 2.5 A. The protein fold consists of a 16-stranded parallel beta-helix with a V-shaped cross-section, and is the largest beta-helix known to date. Several between-strand weakly conserved amino-acid repeats form internal and external ladders. The structure appears as a helix from which several loops protrude, which contain sequence motifs associated with the biological activity of the protein. One particular (GGXXP)5 sequence is located directly after the RGD motif, and may mediate interaction with epithelial cells. The carboxy-terminal region of P.69 pertactin incorporates a (PQP)5 motif loop containing the major immunoprotective epitope.

PubMed: 8609998
DOI: 10.1038/381090a0

実験手法

X-RAY DIFFRACTION (2.5 Å)