Structural insights into Pseudomonas aeruginosaType six secretion system exported effector 8.

Autor: González-Magaña A; Instituto Biofisika (UPV/EHU, CSIC), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, University of the Basque Country, 48940 Leioa, Spain., Sainz-Polo MÁ; Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, 48160 Derio, Spain., Pretre G; Instituto Biofisika (UPV/EHU, CSIC), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, University of the Basque Country, 48940 Leioa, Spain., Çapuni R; Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, 48160 Derio, Spain., Lucas M; Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Consejo Superior de Investigaciones Científicas (CSIC)-Universidad de Cantabria. Santander, 39011 Cantabria, Spain., Altuna J; Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, 48160 Derio, Spain., Montánchez I; Departamento de Inmunología, Microbiología y Parasitología, University of the Basque Country, 48940 Leioa, Spain., Fucini P; Ikerbasque, Basque Foundation for Science, 48013 Bilbao, Spain., Albesa-Jové D; Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, 48160 Derio, Spain; Ikerbasque, Basque Foundation for Science, 48013 Bilbao, Spain. Electronic address: david.albesa@ehu.eus.
Jazyk: angličtina
Zdroj: Journal of structural biology [J Struct Biol] 2020 Dec 01; Vol. 212 (3), pp. 107651. Date of Electronic Publication: 2020 Oct 20.
DOI: 10.1016/j.jsb.2020.107651
Abstrakt: Recent reports indicate that the Type six secretion system exported effector 8 (Tse8) is a cytoactive effector secreted by the Type VI secretion system (T6SS) of the human pathogen Pseudomonas aeruginosa. The T6SS is a nanomachine that assembles inside of the bacteria and injects effectors/toxins into target cells, providing a fitness advantage over competing bacteria and facilitating host colonisation. Here we present the first crystal structure of Tse8 revealing that it conserves the architecture of the catalytic triad Lys84-transSer162-Ser186 that characterises members of the Amidase Signature superfamily. Furthermore, using binding affinity experiments, we show that the interaction of phenylmethylsulfonyl fluoride (PMSF) to Tse8 is dependent on the putative catalytic residue Ser186, providing support for its nucleophilic reactivity. This work thus demonstrates that Tse8 belongs to the Amidase Signature (AS) superfamily. Furthermore, it highlights Tse8 similarity to two family members: the Stenotrophomonas maltophilia Peptide Amidase and the Glutamyl-tRNA Gln amidotransferase subunit A from Staphylococcus aureus.
(Copyright © 2020 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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