6g4h
From Proteopedia
Crystal structure of the periplasmic domain of TgpA from Pseudomonas aeruginosa bound to ethylmercury
Structural highlights
FunctionTGPA_PSEAE Displays transglutaminase activity (TGase) in vitro. Plays a critical role in the viability of P.aeruginosa. Might contribute to an essential function linked to the cell wall.[1] Publication Abstract from PubMedPseudomonas 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 1.6A resolution as a first step towards structure-activity analysis of a new potential target for the discovery of antibacterial compounds. Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa.,Uruburu M, Mastrangelo E, Bolognesi M, Ferrara S, Bertoni G, Milani M J Struct Biol. 2019 Mar 1;205(3):18-25. doi: 10.1016/j.jsb.2018.12.004. Epub 2018, Dec 30. PMID:30599211[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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