8BVP
Crystal structure of an N-terminal fragment of the effector protein Lpg2504 (SidI) from Legionella pneumophila
Summary for 8BVP
| Entry DOI | 10.2210/pdb8bvp/pdb |
| Descriptor | Restriction endonuclease, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | bacterial effector, glycosyl transferase, legionella pneumophila, translation inhibition, protein binding |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 62272.65 |
| Authors | Machtens, D.A.,Willerding, J.M.,Eschenburg, S.,Reubold, T.F. (deposition date: 2022-12-05, release date: 2023-05-03, Last modification date: 2024-11-20) |
| Primary citation | Machtens, D.A.,Willerding, J.M.,Eschenburg, S.,Reubold, T.F. Crystal structure of the N-terminal domain of the effector protein SidI of Legionella pneumophila reveals a glucosyl transferase domain. Biochem.Biophys.Res.Commun., 661:50-55, 2023 Cited by PubMed Abstract: The Gram-negative bacterium Legionella pneumophila is an accidental human pathogen that can cause a life-threatening respiratory infection called Legionellosis. In the course of infection, L. pneumophila injects more than 300 effector proteins into the host cell. The effector proteins modify the intracellular environment in order to create a stable compartment for proliferation within the host cell. The effector protein SidI has been shown to potently inhibit host translation upon translocation. SidI is able to interact with the translation elongation factor eEF1A, which has been hypothesized to be a target of SidI. A postulated glycosyltransferase domain in the C-terminal half may be responsible for the toxic effect of SidI. Here, we present the crystal structure of an N-terminal fragment of SidI containing residues 37-573. The structure is divided into three subdomains, two of which display a novel fold. The third subdomain shows close structural homology to GT-B fold glycosyltransferases. Based on structural analysis we predict that the two previously identified residues R453 and E482 assume roles in the catalytic activity of SidI. Furthermore, we show that the N-terminal fragment of SidI is able to directly interact with a postulated target, the translation elongation factor eEF1A. PubMed: 37087798DOI: 10.1016/j.bbrc.2023.04.029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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