Structure of bacillus subtilis [gamma]-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue

HIGHLIGHTS

• who: Biological and colleagues from the Department Sciences, Graduate School Science, University, Toyonaka, Miyazaki, Miyazaki, Japan have published the Article: Structure of Bacillus subtilis [gamma]-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue, in the Journal: (JOURNAL) of 25/09/2013
• what: The authors report the binding mode of acivicin to B. subtilis GGT at 1.8 Å resolution, showing that acivicin is bound to the O atom of Thr403, the catalytic nucleophile of the enzyme, through its C3 atom. The authors compared . . .
  

   

  

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