Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG.

ABSTRACT: Lipid II, the main component of the bacterial cell wall, is synthesized by the addition of UDP-N-acetylglucosamine to the UDP-N-acetylmuramic acid pentapeptide catalyzed by the glycosyltransferase MurG. Owing to its critical role in cell-wall biosynthesis, MurG is considered to be an attractive target for antibacterial agents. Although the Mur family ligases have been extensively studied, the molecular mechanism of the oligomeric scaffolding assembly of MurG remains unclear. In this study, MurG from Acinetobacter baumannii (abMurG), a human pathogen, was characterized and its hexameric crystal structure was unveiled; this is the first homo-oligomeric structure to be described in the MurG family and the Mur family. Homogeneous protein samples were produced for structura

SUBMITTER: Jung KH 

PROVIDER: S-EPMC8256705 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature