Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP

• Published in: Cell research Vol. 23; no. 6; pp. 775 - 787
• Main Authors: Yu, Qin, Hu, Liyan, Yao, Qing, Zhu, Yongqun, Dong, Na, Wang, Da-Cheng, Shao, Feng
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.06.2013; Nature Publishing Group
• Subjects: 631/45/173; 631/535; 631/80/313; 631/80/313/2011; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - ultrastructure; Biomedical and Life Sciences; Catalytic Domain; Cell Biology; Crystallography, X-Ray; Escherichia coli Proteins - metabolism; GAP; GTPase; GTPase-Activating Proteins - metabolism; Legionella pneumophila; Legionella pneumophila - metabolism; Life Sciences; Mutation; Original; original-article; Pathogens; Protein Folding; Protein Structure, Tertiary; rab1 GTP-Binding Proteins - metabolism; Residues; 催化活性; 军团菌; 模仿; 真核; 结构分析; 谷氨酰胺; TBC GAP; type IV secretion system; GTPase-activating protein (GAP); Rab GTPases; membrane trafficking

Rab GTPases are emerging targets of diverse bacterial pathogens. Here, we perform biochemical and structural analyses of LepB, a Rab GTPase-activating protein （GAP） effector from Legionellapneumophila. We map LepB GAP domain to residues 313-618 and show that the GAP domain is Rabl specific with a ca...