7ETX

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

Summary for 7ETX

• Entry DOI: 10.2210/pdb7etx/pdb
• Descriptor: Tryptophan biosynthesis protein TrpCF, GLYCEROL (3 entities in total)
• Functional Keywords: tryptophan biosynthesis, amino acid, bifunctional, biosynthetic protein
• Biological source: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
• Total number of polymer chains: 1
• Total formula weight: 51788.31

Authors

Prak, W.J.,Kim, K.-J. (deposition date: 2021-05-15, release date: 2022-05-11, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)