7DSM
Anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae
Summary for 7DSM
| Entry DOI | 10.2210/pdb7dsm/pdb |
| Related | 7DSJ |
| Descriptor | Anthranilate phosphoribosyltransferase (2 entities in total) |
| Functional Keywords | glycosyltransferase, transferase, tryptophan biosynthesis, anthranilate phosphoribosyltransferase activity |
| Biological source | Saccharomyces cerevisiae S288C (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 83679.55 |
| Authors | |
| Primary citation | Wu, X.,Zhang, M.,Kuang, Z.,Yue, J.,Xue, L.,Zhu, M.,Zhu, Z.,Khan, M.H.,Niu, L. Crystal structures of anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae. Acta Crystallogr.,Sect.F, 77:61-69, 2021 Cited by PubMed Abstract: Anthranilate phosphoribosyltransferase (AnPRT) catalyzes the transfer of the phosphoribosyl group of 5'-phosphoribosyl-1'-pyrophosphate (PRPP) to anthranilate to form phosphoribosyl-anthranilate. Crystal structures of AnPRTs from bacteria and archaea have previously been determined; however, the structure of Saccharomyces cerevisiae AnPRT (ScAnPRT) still remains unsolved. Here, crystal structures of ScAnPRT in the apo form as well as in complex with its substrate PRPP and the substrate analogue 4-fluoroanthranilate (4FA) are presented. These structures demonstrate that ScAnPRT exhibits the conserved structural fold of type III phosphoribosyltransferase enzymes and shares the similar mode of substrate binding found across the AnPRT protein family. In addition, crystal structures of ScAnPRT mutants (ScAnPRT and ScAnPRT) were also determined. These structures suggested that the conserved residue Ser121 is critical for binding PRPP, while Gly141 is dispensable for binding 4FA. In summary, these structures improved the preliminary understanding of the substrate-binding mode of ScAnPRT and laid foundations for future research. PubMed: 33682790DOI: 10.1107/S2053230X21001989 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.39 Å) |
Structure validation
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