9KN2

Crystallization of zinc metalloproteinase PepO from Porphyromonas gingivalis

9KN2 の概要

• エントリーDOI: 10.2210/pdb9kn2/pdb
• 分子名称: Endopeptidase PepO, N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-LEUCYL-L-TRYPTOPHAN, ZINC ION, ... (5 entities in total)
• 機能のキーワード: zinc metalloproteinase, inhibitor, complex, peptidase m13 family, metal binding protein
• 由来する生物種: Porphyromonas gingivalis W83
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77165.81

構造登録者

Feng, C.Y.,Feng, C.Y. (登録日: 2024-11-18, 公開日: 2025-10-01)

主引用文献

Feng, C.,Yu, W.,Jiang, Y.,Xia, R.
Structural and biochemical characterization of a zinc metallopeptidase from Porphyromonas gingivalis.
Biochem.Biophys.Res.Commun., 744:151201-151201, 2025

PubMed Abstract: The pathogen Porphyromonas gingivalis contributes to the pathogenesis of periodontitis and other systemic diseases. The zinc-dependent metallopeptidase PepO is a virulence factor that plays a crucial role in the adhesion and invasion of Porphyromonas gingivalis to human cells. Here, we solved the 2.04 Å crystal structure of wild-type PepO in complex with the inhibitor phosphoramidon. The active-site pocket of PepO appears to exhibit an increased hydrophobicity and a more pronounced negative charge, highlighting distinct structural features compared to its homologs. In addition to phosphoramidon, several zinc metallopeptidase inhibitors, including thiorphan, omapatrilat, and sacubitrilat, exhibited varying degrees of inhibition on PepO enzymatic activity. Notably, the recombinant PepO showed distinct binding profiles to human fibrinogen, a characteristic that likely contributes to its role as virulence factors. These findings provide significant insights into the structural and functional mechanisms of PepO, offering a platform for the rational design of targeted inhibitors against the periodontal pathogen P. gingivalis.

PubMed: 39709774
DOI: 10.1016/j.bbrc.2024.151201

実験手法

X-RAY DIFFRACTION (2.04 Å)