3NKU
Crystal structure of the N-terminal domain of DrrA/SidM from Legionella pneumophila
Summary for 3NKU
| Entry DOI | 10.2210/pdb3nku/pdb |
| Descriptor | DrrA, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | posttranslational modification, ampylation, adenylylation, rab1b, rab1, drra, sidm, vesicular transport, protein transport |
| Biological source | Legionella pneumophila subsp. pneumophila |
| Total number of polymer chains | 2 |
| Total formula weight | 49359.00 |
| Authors | Mueller, M.P.,Peters, H.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. (deposition date: 2010-06-21, release date: 2010-08-04, Last modification date: 2024-11-20) |
| Primary citation | Muller, M.P.,Peters, H.,Blumer, J.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science, 329:946-949, 2010 Cited by PubMed Abstract: In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active. PubMed: 20651120DOI: 10.1126/science.1192276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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