3KM5

Crystal Structure Analysis of the K2 Cleaved Adhesin Domain of Lys-gingipain (Kgp)

Summary for 3KM5

• Entry DOI: 10.2210/pdb3km5/pdb
• Descriptor: Lysine specific cysteine protease, CALCIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: beta jelly roll barrel, cleaved adhesin family, lys-gingipain, hemagglutination domain, cell invasion
• Biological source: Porphyromonas gingivalis
• Total number of polymer chains: 2
• Total formula weight: 39246.78

Authors

Li, N.,Collyer, C.A.,Hunter, N. (deposition date: 2009-11-09, release date: 2010-03-31, Last modification date: 2024-03-20)

Primary citation

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

PubMed Abstract: Porphyromonas gingivalis is an obligately anaerobic bacterium recognized as an aetiological agent of adult periodontitis. P. gingivalis produces cysteine proteinases, the gingipains. The crystal structure of a domain within the haemagglutinin region of the lysine gingipain (Kgp) is reported here. The domain was named K2 as it is the second of three homologous structural modules in Kgp. The K2 domain structure is a 'jelly-roll' 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. Possible functions of K2 were investigated. K2 induced haemolysis of erythrocytes in a dose-dependent manner that was augmented by the blocking of anion transport. Further, cysteine-activated arginine gingipain RgpB, which degrades glycophorin A, sensitized erythrocytes to the haemolytic effect of K2. Cleaved K2, similar to that found in extracted Kgp, lacks the haemolytic activity indicating that autolysis of Kgp may be a staged process which is artificially enhanced by extraction of the protein. The data indicate a functional role for K2 in the integrated capacity conferred by Kgp to enable the porphyrin auxotroph P. gingivalis to capture essential haem from erythrocytes.

PubMed: 20233299
DOI: 10.1111/j.1365-2958.2010.07123.x

Experimental method

X-RAY DIFFRACTION (1.4 Å)