Virulence protein J domain 1 maintains the canonical α/β-hydrolase fold but is likely to lack a functional catalytic triad, suggesting functional divergence from classical hydrolases of this superfamily #BacterialPathogens #TypeIVSecretionSystem doi.org/10.1107/S205...
September 9, 2025 at 2:50 PM
Virulence protein J domain 1 maintains the canonical α/β-hydrolase fold but is likely to lack a functional catalytic triad, suggesting functional divergence from classical hydrolases of this superfamily #BacterialPathogens #TypeIVSecretionSystem doi.org/10.1107/S205...
Chloé Dugelay et al.: Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus ##BacterialPathogens##EsteraseFold##TypeIVSecretionSystem... ##IUCrhttps://journals.iucr.org/paper?S2053230X25006697
Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus
Virulence protein J (VirJ) is produced by the bacterial pathogen Brucella abortus and contains two domains, D1 and D2. The crystal structure of VirJD1 is presented at a resolution of 1.7 Å and displays an α/β-hydrolase fold with a central β-sheet surrounded by α-helices. Structural comparison with other members of the family suggests that VirJD1 lacks the characteristic catalytic triad.
journals.iucr.org
August 19, 2025 at 12:00 AM
Chloé Dugelay et al.: Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus ##BacterialPathogens##EsteraseFold##TypeIVSecretionSystem... ##IUCrhttps://journals.iucr.org/paper?S2053230X25006697