Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health

Protein Sci. 2015 Jan;24(1):162-6. doi: 10.1002/pro.2589. Epub 2014 Dec 3.

Abstract

The oral pathogen Porphyromonas gingivalis is a keystone pathogen in the development of chronic periodontitis. Gingipains, the principle virulence factors of P. gingivalis are multidomain, cell-surface proteins containing a cysteine protease domain. The lysine specific gingipain, Kgp, is a critical virulence factor of P. gingivalis. We have determined the X-ray crystal structure of the lysine-specific protease domain of Kgp to 1.6 Å resolution. The structure provides insights into the mechanism of substrate specificity and catalysis.

Keywords: Kgp; Porphyromonas gingivalis; gingipains; keystone pathogen; lysine specific protease; periodontitis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / metabolism
  • Bacteroidaceae Infections / microbiology*
  • Bacteroidaceae Infections / prevention & control
  • Crystallography, X-Ray
  • Cysteine Endopeptidases / chemistry*
  • Cysteine Endopeptidases / metabolism
  • Gingipain Cysteine Endopeptidases
  • Humans
  • Models, Molecular
  • Oral Health
  • Porphyromonas gingivalis / chemistry*
  • Porphyromonas gingivalis / metabolism
  • Protein Conformation

Substances

  • Adhesins, Bacterial
  • Gingipain Cysteine Endopeptidases
  • Cysteine Endopeptidases

Associated data

  • PDB/4TKX