Peptidoglycan polymerase function and regulation

Area of Science:

• Microbiology
• Biochemistry
• Structural Biology

Background:

• Bacterial cell wall synthesis relies on glycosyltransferases (GTases) to form peptidoglycan (PG).
• Two distinct GTase families, CAZy GT51 (associated with aPBPs) and CAZy GT119 (SEDS family), are crucial for PG polymerization.
• These GTases catalyze the formation of β-1,4 glycosidic bonds, linking disaccharide subunits of the PG polymer.

Purpose of the Study:

• To review the structure-activity relationship of the two main PG GTase families.
• To elucidate the coordination between GTase and transpeptidase activities.
• To explore regulatory mechanisms controlling these enzymes during bacterial cell growth and division.

Main Methods:

• This review synthesizes existing research on PG GTases.
• Focuses on structural and functional analyses of GT51 and GT119 families.
• Examines their roles within the bacterial elongasome and divisome complexes.

Main Results:

• GT51 family enzymes, often part of bifunctional aPBPs, possess a lysozyme-like domain.
• GT119 family enzymes are polytopic membrane proteins belonging to the SEDS family.
• Multiple GTases from both families operate within a single cell, potentially with overlapping or distinct functions.

Conclusions:

• Understanding the structure-activity relationships and regulation of these PG GTases is vital for comprehending bacterial cell envelope biogenesis.
• These enzymes are key targets for novel antibacterial strategies.