2V2C

The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

2V2C の概要

• エントリーDOI: 10.2210/pdb2v2c/pdb
• 関連するPDBエントリー: 1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 2J27 2V0T 3TIM 4TIM 5TIM 6TIM
• 分子名称: TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, SULFATE ION, 2-PHOSPHOGLYCOLIC ACID, ... (4 entities in total)
• 機能のキーワード: isomerase, glycosome, tim-barrel, glycolysis, engineering, pentose shunt, point mutation, tim, 2pg, a178l, loop6, hinge, loop-6, enzyme, fatty acid biosynthesis, triosephosphate isomerase, gluconeogenesis, lipid synthesis, 2-phospho glycollate
• 由来する生物種: TRYPANOSOMA BRUCEI BRUCEI
• 細胞内の位置: Glycosome: P04789
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27352.13

構造登録者

Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. (登録日: 2007-06-05, 公開日: 2008-02-19, 最終更新日: 2023-12-13)

• 主引用文献: Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K.; Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim.; Acta Crystallogr.,Sect.D, 64:178-, 2008; PubMed: 18219118; DOI: 10.1107/S0907444907059021

実験手法

X-RAY DIFFRACTION (1.89 Å)