7ETX

Crystal structure of bifunctional indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase (TrpC) from corynebacterium glutamicum

7ETX の概要

• エントリーDOI: 10.2210/pdb7etx/pdb
• 分子名称: Tryptophan biosynthesis protein TrpCF, GLYCEROL (3 entities in total)
• 機能のキーワード: tryptophan biosynthesis, amino acid, bifunctional, biosynthetic protein
• 由来する生物種: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51788.31

構造登録者

Prak, W.J.,Kim, K.-J. (登録日: 2021-05-15, 公開日: 2022-05-11, 最終更新日: 2024-10-16)

主引用文献

Park, W.,Son, H.F.,Lee, D.,Kim, I.K.,Kim, K.J.
Crystal Structure and Functional Characterization of the Bifunctional N -(5'-Phosphoribosyl)anthranilate Isomerase-indole-3-glycerol-phosphate Synthase from Corynebacterium glutamicum
J.Agric.Food Chem., 69:12485-12493, 2021

PubMed Abstract: L-Tryptophan is known as an aromatic amino acid and one of the essential amino acids that must be ingested through various additives or food. TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In this report, we identified the crystal structure of TrpCF from (TrpCF) and successfully elucidated the active site by attaching rCdRP similar to the substrate and product of the TrpCF reaction. Also, we revealed that TrpCF shows a conformational change at the loops upon substrate binding. We analyzed amino acid sequences of the homologues of TrpCF, and the residues of the substrate-binding site in TrpCF were highly conserved except for some residues. These less conserved residues were replaced by site-directed mutagenesis experiments. Consequently, we obtained the TrpCF (PRAI) variant that has enhanced activity.

PubMed: 34657425
DOI: 10.1021/acs.jafc.1c05132

実験手法

X-RAY DIFFRACTION (2.1 Å)