Literature summary for 3.4.21.50 extracted from

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 (2015), Protein Sci., 24, 162-166.

Search for more literature for 3.4.21.50

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of Gly681-Ala710 deletion mutant in Porphyromonas gingivalis strain ECR368, release of enzyme Kgp catalytic domain in soluble form into the culture supernatant	Porphyromonas gingivalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 0.001 ml of protein with reservoir solution containing 27% PEG 4000, 100 mM sodium acetate, pH 5.0, and 0.2 M ammonium sulfate, equilibration over 0.5 ml of reservoir solution, one week, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement/heavy atom derivatization	Porphyromonas gingivalis

Crystallization (Comment)

Organism

purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 0.001 ml of protein with reservoir solution containing 27% PEG 4000, 100 mM sodium acetate, pH 5.0, and 0.2 M ammonium sulfate, equilibration over 0.5 ml of reservoir solution, one week, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement/heavy atom derivatization

Porphyromonas gingivalis

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a Gly681-Ala710 deletion mutant	Porphyromonas gingivalis
Q520S	site-directed mutagenesis, the mutant shows altered substrate binding compared to the wild-type enzyme	Porphyromonas gingivalis

Inhibitors

Inhibitors	Comment	Organism	Structure
N-tosyl-L-Lys chloromethyl ketone	TLCK, a covalently Cys477-bound inhibitor	Porphyromonas gingivalis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Porphyromonas gingivalis	9986	-
extracellular	-	Porphyromonas gingivalis	-	-

Organism

Organism	UniProt	Comment	Textmining
Porphyromonas gingivalis	-	gene kgp	-
Porphyromonas gingivalis W50	-	gene kgp	-

Subunits

Subunits	Comment	Organism
More	three-dimensional crystal structure of enzyme Kgp	Porphyromonas gingivalis

Synonyms

Synonyms	Comment	Organism
KGP	-	Porphyromonas gingivalis
lysine specific gingipain	-	Porphyromonas gingivalis
lysine specific protease	-	Porphyromonas gingivalis

General Information

General Information	Comment	Organism
additional information	the enzyme has a hemagglutininadhesin domain in the polypeptide region C-terminal to the catalytic domains, three-dimensional crystal structure of enzyme Kgp. The conserved acidic residue Asp388 may play a role in the catalytic mechanism. A chain of three welldefined water molecules that acts as H-bond acceptors in their interactions with the Nf of the lysine. The other end of this H-bonded chain of water molecules is in turn H-bonded to the backbone carbonyl oxygen of Asp516, structure-function analysis, overview	Porphyromonas gingivalis
physiological function	gingipains, the principle virulence factors of Porphyromonas gingivalis are multidomain, cell-surface proteins containing a cysteine protease domain. The lysine specific gingipain, Kgp, is a critical virulence factor of Porphyromonas gingivalis	Porphyromonas gingivalis