5Y1A

HBP35 of Porphyromonas gingivalis

5Y1A の概要

• エントリーDOI: 10.2210/pdb5y1a/pdb
• 分子名称: 35 kDa hemin binding protein (2 entities in total)
• 機能のキーワード: porphyromonas gingivalis, beta-sandwich domain, thioredoxin domain, electron transport
• 由来する生物種: Porphyromonas gingivalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37605.39

構造登録者

Kakuda, S.,Suzuki, M.,Sato, K. (登録日: 2017-07-20, 公開日: 2018-07-25, 最終更新日: 2024-03-27)

主引用文献

Sato, K.,Kakuda, S.,Yukitake, H.,Kondo, Y.,Shoji, M.,Takebe, K.,Narita, Y.,Naito, M.,Nakane, D.,Abiko, Y.,Hiratsuka, K.,Suzuki, M.,Nakayama, K.
Immunoglobulin-like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system.
Mol. Microbiol., 110:64-81, 2018

PubMed Abstract: The periodontal pathogen Porphyromonas gingivalis secretes many potent virulence factors using the type IX secretion system (T9SS). T9SS cargo proteins that have been structurally determined by X-ray crystallography are composed of a signal peptide, functional domain(s), an immunoglobulin (Ig)-like domain and a C-terminal domain. Role of the Ig-like domains of cargo proteins in the T9SS has not been elucidated. Gingipain proteases, which are cargo proteins of the T9SS, were degraded when their Ig-like domains were lacking or truncated. The degradation was dependent on the activity of a quality control factor, HtrA protease. Another T9SS cargo protein, HBP35, which has a thioredoxin domain as a functional domain, was analyzed by X-ray crystallography, revealing that HBP35 has an Ig-like domain after the thioredoxin domain and that the hydrophobic regions of the thioredoxin domain and the Ig-like domain face each other. HBP35 with substitution of hydrophobic amino acids in the Ig-like domain was degraded depending on HtrA. These results suggest that the Ig-like domain mediates stability of the cargo proteins in the T9SS.

PubMed: 30030863
DOI: 10.1111/mmi.14083

実験手法

X-RAY DIFFRACTION (1.8 Å)