6ZQ7
Crystal structure of Chaetomium thermophilum Glycerol Kinase in I222 space group
Summary for 6ZQ7
| Entry DOI | 10.2210/pdb6zq7/pdb |
| Descriptor | Glycerol kinase-like protein, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | kinase, glycerol, metabolism, transferase |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 1 |
| Total formula weight | 57221.44 |
| Authors | Wilk, P.,Wator, E.,Grudnik, P. (deposition date: 2020-07-09, release date: 2020-12-23, Last modification date: 2024-01-31) |
| Primary citation | 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 Cited by 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: 33339113DOI: 10.3390/ijms21249570 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.421 Å) |
Structure validation
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