6G4H
Crystal structure of the periplasmic domain of TgpA from Pseudomonas aeruginosa bound to ethylmercury
Summary for 6G4H
| Entry DOI | 10.2210/pdb6g4h/pdb |
| Related | 6G49 |
| Descriptor | Protein-glutamine gamma-glutamyltransferase, PHOSPHATE ION, ETHYL MERCURY ION, ... (4 entities in total) |
| Functional Keywords | essential bacterial protein, transferase |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 39051.66 |
| Authors | Milani, M.,Mastrangelo, E.,Uruburu, M. (deposition date: 2018-03-27, release date: 2019-04-10, Last modification date: 2024-05-08) |
| Primary citation | Uruburu, M.,Mastrangelo, E.,Bolognesi, M.,Ferrara, S.,Bertoni, G.,Milani, M. Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa. J.Struct.Biol., 205:18-25, 2019 Cited by PubMed Abstract: Pseudomonas aeruginosa is an opportunistic pathogen associated with severe diseases, such as cystic fibrosis. During an extensive search for novel essential genes, we identified tgpA (locus PA2873) in P. aeruginosa PAO1, as a gene playing a critical role in bacterial viability. TgpA, the translated protein, is an internal membrane protein with a periplasmic soluble domain, predicted to be endowed with a transglutaminase-like fold, hosting the Cys404, His448, and Asp464 triad. We report here that Cys404 mutation hampers the essential role of TgpA in granting P. aeruginosa viability. Moreover, we present the crystal structure of the TgpA periplasmic domain at 1.6 Å resolution as a first step towards structure-activity analysis of a new potential target for the discovery of antibacterial compounds. PubMed: 30599211DOI: 10.1016/j.jsb.2018.12.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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