6R2N

Crystal structure of KlGlk1 glucokinase from Kluyveromyces lactis

Summary for 6R2N

• Entry DOI: 10.2210/pdb6r2n/pdb
• Descriptor: Glucokinase-1, 1,2-ETHANEDIOL, BROMIDE ION, ... (4 entities in total)
• Functional Keywords: kluyveromyces lactis, glucokinase, sugar metabolism, transferase
• Biological source: Kluyveromyces lactis
• Total number of polymer chains: 3
• Total formula weight: 160243.53

Authors

Zak, K.,Wator, E.,Grudnik, P. (deposition date: 2019-03-18, release date: 2019-10-16, Last modification date: 2024-01-24)

Primary citation

Zak, K.M.,Kalinska, M.,Wator, E.,Kuska, K.,Krutyholowa, R.,Dubin, G.,Popowicz, G.M.,Grudnik, P.
Crystal Structure of Kluyveromyces lactis Glucokinase ( Kl Glk1).
Int J Mol Sci, 20:-, 2019

PubMed Abstract: Glucose phosphorylating enzymes are crucial in the regulation of basic cellular processes, including metabolism and gene expression. Glucokinases and hexokinases provide a pool of phosphorylated glucose in an adenosine diphosphate (ADP)- and ATP-dependent manner to shape the cell metabolism. The glucose processing enzymes from are poorly characterized despite the emerging contribution of this yeast strain to industrial and laboratory scale biotechnology. The first reports on glucokinase (Glk1) positioned the enzyme as an essential component required for glucose signaling. Nevertheless, no biochemical and structural information was available until now. Here, we present the first crystal structure of Glk1 together with biochemical characterization, including substrate specificity and enzyme kinetics. Additionally, comparative analysis of the presented structure and the prior structures of hexokinase (Hxk1) demonstrates the potential transitions between open and closed enzyme conformations upon ligand binding.

PubMed: 31569356
DOI: 10.3390/ijms20194821

Experimental method

X-RAY DIFFRACTION (2.596 Å)