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J Am Chem Soc. 2017 Dec 13;139(49):17727-17730. doi: 10.1021/jacs.7b10170. Epub 2017 Nov 30.

Identification of a Functionally Unique Family of Penicillin-Binding Proteins.

Author information

1
Department of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
2
Department of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.
3
Department of Ophthalmology, Harvard Medical School, Massachusetts Eye and Ear Infirmary , Boston, Massachusetts 02114, United States.

Abstract

Penicillin-binding proteins (PBPs) are enzymes involved in the assembly of the bacterial cell wall, a major target for antibiotics. These proteins are classified by mass into high-molecular-weight PBPs, which are transpeptidases that form peptidoglycan cross-links, and low-molecular-weight PBPs, which are typically hydrolases. We report a functionally unique family of low-molecular-weight PBPs that act as transpeptidases rather than hydrolases, but they do not cross-link peptidoglycan. We show that these PBPs can exchange d-amino acids bearing chemical tags or affinity handles into peptidoglycan precursors, including Lipid II, enabling biochemical studies of proteins involved in cell wall assembly. We report that, in two organisms, the PBPs incorporate lysine into cellular peptidoglycan and that, further, the PBPs have the unprecedented ability to transfer the primary ε-amine of lysine to peptidoglycan.

PMID:
29182854
PMCID:
PMC5729098
DOI:
10.1021/jacs.7b10170
[Indexed for MEDLINE]
Free PMC Article

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