Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa
Articolo
Data di Pubblicazione:
2019
Citazione:
Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa / M. Uruburu, E. Mastrangelo, M. Bolognesi, S. Ferrara, G. Bertoni, M. Milani. - In: JOURNAL OF STRUCTURAL BIOLOGY. - ISSN 1047-8477. - 205:3(2019 Mar 01), pp. 18-25. [10.1016/j.jsb.2018.12.004]
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Antibacterials; Cystic fibrosis; Heterologous expression; Peptidoglycans; Periplasmic proteins; Point mutations; X-ray crystallography; Structural Biology
Elenco autori:
M. Uruburu, E. Mastrangelo, M. Bolognesi, S. Ferrara, G. Bertoni, M. Milani
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