An asymmetric structure of bacterial trprs supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening

HIGHLIGHTS

• who: Manli Xiang and collaborators from the Guangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery and Research Center for Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, Guangdong, China have published the research work: An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening, in the Journal: (JOURNAL)
• what: In this study, the cocrystal_structure of niraparib bound to the asymmetric EcTrpRS was determined to 2.10 Au030a resolution . The u2018open-closed` asymmetric structure of EcTrpRS determined in this study provides a good . . .
  

   

  

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