4U06

Structure of Leptospira interrogans LRR protein LIC10831

4U06 の概要

• エントリーDOI: 10.2210/pdb4u06/pdb
• 関連するPDBエントリー: 4TZH 4U08 4U09
• 分子名称: LIC10831, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: unknown function, lrr protein, pathogen, virulence factor
• 由来する生物種: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40777.65

構造登録者

Shepard, W.,Saul, F.A.,Haouz, A.,Picardeau, M. (登録日: 2014-07-11, 公開日: 2015-06-03, 最終更新日: 2024-11-13)

主引用文献

Miras, I.,Saul, F.,Nowakowski, M.,Weber, P.,Haouz, A.,Shepard, W.,Picardeau, M.
Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans.
Acta Crystallogr.,Sect.D, 71:1351-1359, 2015

PubMed Abstract: Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic α/β-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria.

PubMed: 26057675
DOI: 10.1107/S139900471500704X

実験手法

X-RAY DIFFRACTION (1.9 Å)