Premium
Structure of the lysine specific protease K gp from P orphyromonas gingivalis , a target for improved oral health
Author(s) -
Gorman Michael A.,
Seers Christine A.,
Michell Belinda J.,
Feil Susanne C.,
Huq N. Laila,
Cross Keith J.,
Reynolds Eric C.,
Parker Michael W.
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2589
Subject(s) - porphyromonas gingivalis , virulence , protease , cysteine protease , virulence factor , microbiology and biotechnology , pathogen , chemistry , lysine , biology , amino acid , biochemistry , bacteria , enzyme , gene , genetics
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.