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6YHV

Structural insights into Pseudomonas aeruginosa Type six secretion system exported effector 8: unliganded Tse8

Summary for 6YHV
Entry DOI10.2210/pdb6yhv/pdb
Related6TE4
DescriptorTse8, COPPER (II) ION (3 entities in total)
Functional Keywordsamidase signature (as) superfamily complex, toxin
Biological sourcePseudomonas aeruginosa PAO1
Total number of polymer chains2
Total formula weight127098.18
Authors
Sainz-Polo, M.A.,Capuni, R.,Pretre, G.,Gonzalez-Magana, A.,Lucas, M.,Altuna, J.,Montanchez, I.,Fucini, P.,Albesa-Jove, D. (deposition date: 2020-03-31, release date: 2020-11-04, Last modification date: 2024-01-24)
Primary citationGonzalez-Magana, A.,Sainz-Polo, M.A.,Pretre, G.,Capuni, R.,Lucas, M.,Altuna, J.,Montanchez, I.,Fucini, P.,Albesa-Jove, D.
Structural insights into Pseudomonas aeruginosaType six secretion system exported effector 8.
J.Struct.Biol., 212:107651-107651, 2020
Cited by
PubMed 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-tRNA amidotransferase subunit A from Staphylococcus aureus.
PubMed: 33096229
DOI: 10.1016/j.jsb.2020.107651
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.893 Å)
Structure validation

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