5DHM

Crystal structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis

5DHM の概要

• エントリーDOI: 10.2210/pdb5dhm/pdb
• 分子名称: Immunoreactive 32 kDa antigen (3 entities in total)
• 機能のキーワード: fimbria, adhesin, periodontitis, cell adhesion
• 由来する生物種: Porphyromonas gingivalis ATCC 33277; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75905.25

構造登録者

Kloppsteck, P.,Hall, M.,Persson, K. (登録日: 2015-08-31, 公開日: 2016-04-06, 最終更新日: 2024-10-23)

主引用文献

Kloppsteck, P.,Hall, M.,Hasegawa, Y.,Persson, K.
Structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis in its precursor form: implications for a donor-strand complementation mechanism.
Sci Rep, 6:22945-22945, 2016

PubMed Abstract: Gingivitis and periodontitis are chronic inflammatory diseases that can lead to tooth loss. One of the causes of these diseases is the Gram-negative Porphyromonas gingivalis. This periodontal pathogen is dependent on two fimbriae, FimA and Mfa1, for binding to dental biofilm, salivary proteins, and host cells. These fimbriae are composed of five proteins each, but the fimbriae assembly mechanism and ligands are unknown. Here we reveal the crystal structure of the precursor form of Mfa4, one of the accessory proteins of the Mfa1 fimbria. Mfa4 consists of two β-sandwich domains and the first part of the structure forms two well-defined β-strands that run over both domains. This N-terminal region is cleaved by gingipains, a family of proteolytic enzymes that encompass arginine- and lysine-specific proteases. Cleavage of the N-terminal region generates the mature form of the protein. Our structural data allow us to propose that the new N-terminus of the mature protein may function as a donor strand in the polymerization of P. gingivalis fimbriae.

PubMed: 26972441
DOI: 10.1038/srep22945

実験手法

X-RAY DIFFRACTION (1.9 Å)