3KM5
Crystal Structure Analysis of the K2 Cleaved Adhesin Domain of Lys-gingipain (Kgp)
3KM5 の概要
| エントリーDOI | 10.2210/pdb3km5/pdb |
| 分子名称 | Lysine specific cysteine protease, CALCIUM ION, SULFATE ION, ... (6 entities in total) |
| 機能のキーワード | beta jelly roll barrel, cleaved adhesin family, lys-gingipain, hemagglutination domain, cell invasion |
| 由来する生物種 | Porphyromonas gingivalis |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 39246.78 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 20233299DOI: 10.1111/j.1365-2958.2010.07123.x 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.4 Å) |
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