4tkx | pdb_00004tkx

Structure of Protease

spinqualitylabelsall models 4tkx, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tkx is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, EDO, K, NA, PB, SO4, TCK Activity: Gingipain K, with EC number 3.4.22.47 Resources: FirstGlance, OCA, RCSB, PDBsum Function [KGP83_PORGN] Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).[UniProtKB:B2RLK2] Publication Abstract from PubMed 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 A resolution. The structure provides insights into the mechanism of substrate specificity and catalysis. Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health.,Gorman MA, Seers CA, Michell BJ, Feil SC, Huq NL, Cross KJ, Reynolds EC, Parker MW Protein Sci. 2015 Jan;24(1):162-6. doi: 10.1002/pro.2589. Epub 2014 Dec 3. PMID:25327141 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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