Structural highlights
Function
Q8CM62_STRMG
Publication Abstract from PubMed
Sortase A (SrtA) from Gram positive pathogens is an attractive target for inhibitors due to its role in the attachment of surface proteins to the cell wall. We found that the plant natural product trans-chalcone inhibits Streptococcus mutans SrtA in vitro and also inhibited S. mutans biofilm formation. Mass spectrometry revealed that the trans-chalcone forms a Michael addition adduct with the active site cysteine. The X-ray crystal structure of the SrtA H139A mutant provided new insights into substrate recognition by the sortase family. Our study suggests that chalcone flavonoids have potential as sortase-specific oral biofilm inhibitors.
Molecular basis of Streptococcus mutans sortase A inhibition by the flavonoid natural product trans-chalcone.,Wallock-Richards DJ, Marles-Wright J, Clarke DJ, Maitra A, Dodds M, Hanley B, Campopiano DJ Chem Commun (Camb). 2015 Jun 16;51(52):10483-5. doi: 10.1039/c5cc01816a. PMID:26029850[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wallock-Richards DJ, Marles-Wright J, Clarke DJ, Maitra A, Dodds M, Hanley B, Campopiano DJ. Molecular basis of Streptococcus mutans sortase A inhibition by the flavonoid natural product trans-chalcone. Chem Commun (Camb). 2015 Jun 16;51(52):10483-5. doi: 10.1039/c5cc01816a. PMID:26029850 doi:http://dx.doi.org/10.1039/c5cc01816a
