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Structural insights into Pseudomonas aeruginosa Type six secretion system exported effector 8

Abstract: 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-tRNAGln amidotransferase subunit A from Staphylococcus aureus.

 Fuente: Journal of Structural Biology.Volume 212, Issue 3, 1 December 2020, 107651

 Publisher: Elsevier Science Direct

 Year of publication: 2020

 No. of pages: 10

 Publication type: Article

 DOI: 10.1016/j.jsb.2020.107651

 ISSN: 1047-8477,1095-8657

 Spanish project: CTQ2016-76941-R, CTQ2017-82222-R

Authorship

GONZÁLEZ MAGAÑA, AMAIA

SAÍNZ POLO, MARÍA ANGELA

PRETRE, GABRIELA

ÇAPUNI, RETINA

ALTUNA, JON

MONTANCHEZ, ITXASO

FUCINI, PAOLA

ALBESA JOVÉ, DAVID