Literature summary for 3.4.22.47 extracted from

Li, N.; Yun, P.; Nadkarni, M.; Ghadikolaee, N.; Nguyen, K.; Lee, M.; Hunter, N.; Collyer, C.
Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis (2010), Mol. Microbiol., 76, 861-873.

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Cloned(Commentary)

Cloned (Comment)	Organism
the gene fragment encoding the K2 domain (Ala1157-Gly1334) of Kgp from Porphyromonas gingivalis W83 is cloned into a modified vector pET-32a. The constructed plasmid is transformed into Escherichia coli BL21(DE3) competent cells for protein expression	Porphyromonas gingivalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of a domain within the haemagglutinin region of Kgp is reported here. The K2 domain structure is a jellyroll fold with two anti-parallel beta-sheets. This fold topology is shared with adhesive domains from functionally diverse receptors such as MAM domains, ephrin receptor ligand binding domains and a number of carbohydrate binding modules	Porphyromonas gingivalis

Organism

Organism	UniProt	Comment	Textmining
Porphyromonas gingivalis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography and gel filtration	Porphyromonas gingivalis

Synonyms

Synonyms	Comment	Organism
KGP	-	Porphyromonas gingivalis
Lys-gingipain	-	Porphyromonas gingivalis

General Information

General Information	Comment	Organism
physiological function	the K2 domain of KgP induces haemolysis of erythrocytes in a dose-dependent manner that is augmented by the blocking of anion transport	Porphyromonas gingivalis

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Release 2023.1 (January 2023)