5LHE

Phosphoribosyl anthranilate isomerase from Thermococcus kodakaraensis

5LHE の概要

• エントリーDOI: 10.2210/pdb5lhe/pdb
• 分子名称: N-(5'-phosphoribosyl)anthranilate isomerase, SODIUM ION (3 entities in total)
• 機能のキーワード: tryptophan biosynthesis, tim barrel, protein stability, isomerase
• 由来する生物種: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22994.40

構造登録者

Perveen, S.,Rashid, N.,Papageorgiou, A.C. (登録日: 2016-07-11, 公開日: 2016-11-09, 最終更新日: 2024-01-10)

主引用文献

Perveen, S.,Rashid, N.,Papageorgiou, A.C.
Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis.
Acta Crystallogr F Struct Biol Commun, 72:804-812, 2016

PubMed Abstract: A phosphoribosyl anthranilate isomerase, TkTrpF, from Thermococcus kodakaraensis was expressed in Escherichia coli and purified to homogeneity. TkTrpF was crystallized and its structure was determined by molecular replacement in two different space groups (C2 and P1) using data to 1.85 and 1.75 Å resolution, respectively. TkTrpF belongs to the class of TIM-barrel proteins. Structural comparison with other phosphoribosyl anthranilate isomerases (TrpFs) showed the highest structural similarity to Pyrococcus furiosus TrpF. Similarly to P. furiosus TrpF, TkTrpF is a monomer in solution, in contrast to other thermophilic enzymes, which exist as functional dimers. Although in space group P1 TkTrpF crystallizes with two molecules in the asymmetric unit, the interface is highly improbable in solution. Potential factors for the thermostability of TkTrpF were attributed to an increase in helical structure, an increased number of charged residues and an increase in the number of salt bridges.

PubMed: 27827353
DOI: 10.1107/S2053230X16015223

実験手法

X-RAY DIFFRACTION (1.85 Å)