4TKX

Structure of Protease

Summary for 4TKX

• Entry DOI: 10.2210/pdb4tkx/pdb
• Related PRD ID: PRD_000459
• Descriptor: Lys-gingipain W83, SULFATE ION, SODIUM ION, ... (9 entities in total)
• Functional Keywords: cysteine protease, gingivalis, kgp, co-valent inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Porphyromonas gingivalis
• Cellular location: Lys-gingipain catalytic subunit: Secreted, extracellular space . 39 kDa adhesin: Secreted, extracellular space . 15 kDa adhesin: Secreted, extracellular space . 44 kDa adhesin: Secreted, extracellular space : Q51817
• Total number of polymer chains: 1
• Total formula weight: 51589.74

Authors

Gorman, M.A.,Parker, M.W. (deposition date: 2014-05-28, release date: 2014-12-31, Last modification date: 2024-11-06)

Primary citation

Gorman, M.A.,Seers, C.A.,Michell, B.J.,Feil, S.C.,Huq, N.L.,Cross, K.J.,Reynolds, E.C.,Parker, M.W.
Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health.
Protein Sci., 24:162-166, 2015

PubMed 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.

PubMed: 25327141
DOI: 10.1002/pro.2589

Experimental method

X-RAY DIFFRACTION (1.6 Å)