3WHR
Crystal structure of gamma-glutamyltranspeptidase from Bacillus subtilis (crystal soaked for 3min. in acivicin soln. )
Summary for 3WHR
| Entry DOI | 10.2210/pdb3whr/pdb |
| Related | 2V36 3WHQ 3WHS |
| Descriptor | Gamma-glutamyltranspeptidase large chain, Gamma-glutamyltranspeptidase small chain (3 entities in total) |
| Functional Keywords | glutathione hydrolysis, hydrolase, transferase |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 2 |
| Total formula weight | 66316.09 |
| Authors | Ida, T.,Suzuki, H.,Fukuyama, K.,Hiratake, J.,Wada, K. (deposition date: 2013-08-30, release date: 2014-02-19, Last modification date: 2023-11-08) |
| Primary citation | Ida, T.,Suzuki, H.,Fukuyama, K.,Hiratake, J.,Wada, K. 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. Acta Crystallogr.,Sect.D, 70:607-614, 2014 Cited by PubMed Abstract: γ-Glutamyltranspeptidase (GGT) is an enzyme that plays a central role in glutathione metabolism, and acivicin is a classical inhibitor of GGT. Here, the structure of acivicin bound to Bacillus subtilis GGT determined by X-ray crystallography to 1.8 Å resolution is presented, in which it binds to the active site in a similar manner to that in Helicobacter pylori GGT, but in a different binding mode to that in Escherichia coli GGT. In B. subtilis GGT, acivicin is bound covalently through its C3 atom with sp2 hybridization to Thr403 Oγ, the catalytic nucleophile of the enzyme. The results show that acivicin-binding sites are common, but the binding manners and orientations of its five-membered dihydroisoxazole ring are diverse in the binding pockets of GGTs. PubMed: 24531494DOI: 10.1107/S1399004713031222 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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