1LK5

Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii

1LK5 の概要

• エントリーDOI: 10.2210/pdb1lk5/pdb
• 関連するPDBエントリー: 1LK7
• 分子名称: D-Ribose-5-Phosphate Isomerase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta structure, isomerase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 101157.35

構造登録者

Ishikawa, K.,Matsui, I.,Payan, F.,Cambillau, C.,Ishida, H.,Kawarabayasi, Y.,Kikuchi, H.,Roussel, A. (登録日: 2002-04-24, 公開日: 2002-07-03, 最終更新日: 2024-03-13)

主引用文献

Ishikawa, K.,Matsui, I.,Payan, F.,Cambillau, C.,Ishida, H.,Kawarabayasi, Y.,Kikuchi, H.,Roussel, A.
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.
Structure, 10:877-886, 2002

PubMed Abstract: A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI) is of particular metabolic importance since it catalyzes the interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.

PubMed: 12057201
DOI: 10.1016/S0969-2126(02)00779-7

実験手法

X-RAY DIFFRACTION (1.75 Å)