7DSP

Anthranilate phosphoribosyltransferase variant Ser121Ala from Saccharomyces cerevisiae with Mg bound

7DSP の概要

• エントリーDOI: 10.2210/pdb7dsp/pdb
• 関連するPDBエントリー: 7DSJ
• 分子名称: Anthranilate phosphoribosyltransferase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: glycosyltransferase, transferase, tryptophan biosynthesis, anthranilate phosphoribosyltransferase activity
• 由来する生物種: Saccharomyces cerevisiae S288C (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83696.16

構造登録者

Wu, X. (登録日: 2020-12-31, 公開日: 2021-03-17, 最終更新日: 2023-11-29)

主引用文献

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

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: 33682790
DOI: 10.1107/S2053230X21001989

実験手法

X-RAY DIFFRACTION (1.95 Å)