Molecular characterization of the type VI secretion system effector Tlde1a reveals a structurally altered LD-transpeptidase fold.

ABSTRACT: The type VI secretion system (T6SS) is a molecular machine that Gram-negative bacteria have adapted for multiple functions, including interbacterial competition. Bacteria use the T6SS to deliver protein effectors into adjacent cells to kill rivals and establish niche dominance. Central to T6SS-mediated bacterial competition is an arms race to acquire diverse effectors to attack and neutralize target cells. The peptidoglycan has a central role in bacterial cell physiology, and effectors that biochemically modify peptidoglycan structure effectively induce cell death. One such T6SS effector is Tlde1a from Salmonella Typhimurium. Tlde1a functions as an LD-carboxypeptidase to cleave tetrapeptide stems and as an LD-transpeptidase to exchange the terminal D-alanine of a tetrapeptide stem with a n

SUBMITTER: Lorente Cobo N 

PROVIDER: S-EPMC9638812 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature