6ZQ5

Crystal structure of Chaetomium thermophilum Glycerol Kinase in P2221 space group

6ZQ5 の概要

• エントリーDOI: 10.2210/pdb6zq5/pdb
• 分子名称: Glycerol kinase-like protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: kinase, glycerol, metabolism, transferase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114631.10

構造登録者

Wilk, P.,Wator, E.,Malecki, P.,Grudnik, P. (登録日: 2020-07-09, 公開日: 2020-12-23, 最終更新日: 2024-01-31)

主引用文献

Wilk, P.,Kuska, K.,Wator, E.,Malecki, P.H.,Wos, K.,Tokarz, P.,Dubin, G.,Grudnik, P.
Structural Characterization of Glycerol Kinase from the Thermophilic Fungus Chaetomium thermophilum .
Int J Mol Sci, 21:-, 2020

PubMed Abstract: Glycerol is an organic compound that can be utilized as an alternative source of carbon by various organisms. One of the ways to assimilate glycerol by the cell is the phosphorylative catabolic pathway in which its activation is catalyzed by glycerol kinase (GK) and glycerol-3-phosphate (G3P) is formed. To date, several GK crystal structures from bacteria, archaea, and unicellular eukaryotic parasites have been solved. Herein, we present a series of crystal structures of GK from (CtGK) in apo and glycerol-bound forms. In addition, we show the feasibility of an ADP-dependent glucokinase (ADPGK)-coupled enzymatic assay to measure the CtGK activity. New structures described in our work provide structural insights into the GK catalyzed reaction in the filamentous fungus and set the foundation for understanding the glycerol metabolism in eukaryotes.

PubMed: 33339113
DOI: 10.3390/ijms21249570

実験手法

X-RAY DIFFRACTION (2.14 Å)