6V2N

Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys254Ser

「6CU4」から置き換えられました

6V2N の概要

• エントリーDOI: 10.2210/pdb6v2n/pdb
• 分子名称: Phosphoenolpyruvate carboxykinase (ATP), CALCIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: lyase, enzyme, pepcarboxykinase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59531.85

構造登録者

Sokaribo, A.S.,Cotelesage, J.H.,Novakovski, B.,Goldie, H.,Sanders, D. (登録日: 2019-11-25, 公開日: 2019-12-25, 最終更新日: 2023-10-11)

主引用文献

Sokaribo, A.,Novakovski, B.A.A.,Cotelesage, J.,White, A.P.,Sanders, D.,Goldie, H.
Kinetic and structural analysis of Escherichia coli phosphoenolpyruvate carboxykinase mutants.
Biochim Biophys Acta Gen Subj, 1864:129517-129517, 2020

PubMed Abstract: Phosphoenolpyruvate carboxykinase (PEPCK) is a metabolic enzyme in the gluconeogenesis pathway, where it catalyzes the reversible conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) and CO. The substrates for Escherichia coli PEPCK are OAA and MgATP, with Mn acting as a cofactor. Analysis of PEPCK structures have revealed amino acid residues involved in substrate/cofactor coordination during catalysis.

PubMed: 31911238
DOI: 10.1016/j.bbagen.2020.129517

実験手法

X-RAY DIFFRACTION (1.65 Å)