4I1M
Crystal structure of the Legionella pneumophila GAP domain of LepB
Summary for 4I1M
| Entry DOI | 10.2210/pdb4i1m/pdb |
| Related | 4I1O |
| Descriptor | LepB, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | rabgap, hydrolase activator, rab1b, lpg2490, gtpase-activating proteins, hydrolysis, rab1 hydrolase, gtp hydrolase, hydrolase |
| Biological source | Legionella pneumophila subsp. pneumophila |
| Total number of polymer chains | 3 |
| Total formula weight | 102501.86 |
| Authors | Streller, A.,Gazdag, E.M.,Vetter, I.R.,Goody, R.S.,Itzen, A. (deposition date: 2012-11-21, release date: 2013-01-16, Last modification date: 2024-02-28) |
| 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 Cited by 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: 23288104DOI: 10.1038/embor.2012.211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.804 Å) |
Structure validation
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