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

Samir Olatunji, Katherine Bowen, Chia-Ying Huang, Dietmar Weichert, Warispreet Singh, Irina G. Tikhonova, Eoin M. Scanlan, Vincent Olieric and Martin Caffrey ()
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Samir Olatunji: Trinity College Dublin
Katherine Bowen: Trinity College Dublin
Chia-Ying Huang: Swiss Light Source, Paul Scherrer Institute
Dietmar Weichert: Trinity College Dublin
Warispreet Singh: Queen’s University Belfast
Irina G. Tikhonova: Queen’s University Belfast
Eoin M. Scanlan: Trinity College Dublin
Vincent Olieric: Swiss Light Source, Paul Scherrer Institute
Martin Caffrey: Trinity College Dublin

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: 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. The reaction involves acyl transfer from the sn-2 position of the glyceryl moiety to the amino group on the N-terminal cysteine of the substrate via an 8-membered ring intermediate. Transacylation takes place in a confined aromatic residue-rich environment that likely evolved to bring distant moieties on the substrate into proximity and proper orientation for catalysis.

Date: 2021
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DOI: 10.1038/s41467-021-24475-0

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