4I1O

Crystal structure of the Legionella pneumophila GAP domain of LepB in complex with Rab1b bound to GDP and BeF3

Summary for 4I1O

• Entry DOI: 10.2210/pdb4i1o/pdb
• Related: 4I1M
• Descriptor: Ras-related protein Rab-1B, LepB, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: gap, rabgap, hydrolase activator, rab1b, lpg2490, gtpase-activating proteins, hydrolysis, rab1 hydrolase, gtp hydrolase, protein transport-hydrolase complex, protein transport/hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Lipid-anchor; Cytoplasmic side: Q9H0U4
• Total number of polymer chains: 8
• Total formula weight: 221227.36

Authors

Gazdag, E.M.,Streller, A.,Vetter, I.R.,Goody, R.S.,Itzen, A. (deposition date: 2012-11-21, release date: 2013-01-16, Last modification date: 2023-09-20)

Primary citation

Mihai Gazdag, E.,Streller, A.,Haneburger, I.,Hilbi, H.,Vetter, I.R.,Goody, R.S.,Itzen, A.
Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB.
Embo Rep., 14:199-205, 2013

PubMed Abstract: Legionella pneumophila is an intracellularly surviving pathogen that releases about 270 different proteins into the host cell during infection. A set of secreted proteins takes control of the vesicular trafficking regulator Rab1. Legionella LepB inactivates Rab1 by acting as a GTPase-activating protein (GAP). We present the crystal structure of the Rab1b:LepB complex together with a thorough biochemical analysis and show that the GAP domain of LepB consists of an unusual fold. LepB acts by an atypical RabGAP mechanism that is reminiscent of classical GAPs and therefore sets the protein apart from mammalian TBC-like GAPs. Surprisingly, LepB can function as a GAP for Rab3, Rab8, Rab13 and Rab35, too, suggesting that it has a broader cellular role than previously thought.

PubMed: 23288104
DOI: 10.1038/embor.2012.211

Experimental method

X-RAY DIFFRACTION (2.701 Å)