Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis

(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID

Gamma-glutamyltranspeptidase (Ggt) Large subunit

Gamma-glutamyltranspeptidase (Ggt) Small subunit

200 MM HEPES, 25% PEG MME2000, 5 MG/ML PROTEIN, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Gamma-glutamyltranspeptidase (Ggt) Large subunit, Gamma-glutamyltranspeptidase (Ggt) Small subunit (E.C.2.3.22.-)

The enzyme is a heterotetramer generated by the autocatalytic cleavage of the proenzyme.

NTN-HYDROLASE, GLUTAMYLTRANSPEPTIDASE, TRANSFERASE