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Anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae in complex with PRPP and Mg
Structural highlights
FunctionTRPD_YEAST Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA), the second step in tryptophan biosynthesis.[1] Publication Abstract from PubMedAnthranilate 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(Ser121Ala) and ScAnPRT(Gly141Asn)) 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. Crystal structures of anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae.,Wu X, Zhang M, Kuang Z, Yue J, Xue L, Zhu M, Zhu Z, Khan MH, Niu L Acta Crystallogr F Struct Biol Commun. 2021 Mar 1;77(Pt 3):61-69. doi:, 10.1107/S2053230X21001989. Epub 2021 Mar 3. PMID:33682790[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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