Structural basis for the hydrolytic activity of the transpeptidase-like protein DpaA to detach Braun's lipoprotein from peptidoglycan

mBio. 2023 Oct 31;14(5):e0137923. doi: 10.1128/mbio.01379-23. Epub 2023 Oct 13.

Abstract

Cross-linking reaction of Braun's lipoprotein (Lpp) to peptidoglycan (PG) is catalyzed by some members of the YkuD family of transpeptidases. However, the exact opposite reaction of cleaving the Lpp-PG cross-link is performed by DpaA, which is also a YkuD-like protein. In this work, we determined the crystal structure of DpaA to provide the molecular rationale for the ability of the transpeptidase-like protein to cleave, rather than form, the Lpp-PG linkage. Our findings also revealed the structural features that distinguish the different functional types of the YkuD family enzymes from one another.

Keywords: Braun's lipoprotein; DpaA; amidase; peptidoglycan.

MeSH terms

  • Cell Wall / metabolism
  • Lipoproteins / metabolism
  • Peptidoglycan / metabolism
  • Peptidyl Transferases* / metabolism

Substances

  • Peptidyl Transferases
  • Peptidoglycan
  • Lipoproteins