Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis.

ABSTRACT: Lipoproteins serve diverse functions in the bacterial cell and some are essential for survival. Some lipoproteins are adjuvants eliciting responses from the innate immune system of the host. The growing list of membrane enzymes responsible for lipoprotein synthesis includes the recently discovered lipoprotein intramolecular transacylase, Lit. Lit creates a lipoprotein that is less immunogenic, possibly enabling the bacteria to gain a foothold in the host by stealth. Here, we report the crystal structure of the Lit enzyme from Bacillus cereus and describe its mechanism of action. Lit consists of four transmembrane helices with an extracellular cap. Conserved residues map to the cap-membrane interface. They include two catalytic histidines that function to effect unimolecular transacylation.

SUBMITTER: Olatunji S 

PROVIDER: S-EPMC8275575 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature