7E6I

Glucose-6-phosphate dehydrogenase in complex with its substrate glucose-6-phosphate

Summary for 7E6I

• Entry DOI: 10.2210/pdb7e6i/pdb
• Descriptor: Glucose-6-phosphate 1-dehydrogenase, 6-O-phosphono-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: glucose-6-phosphate, dehydrogenase, pentose phosphate pathway, kluyveromyces lactis, oxidoreductase
• Biological source: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast)
• Total number of polymer chains: 1
• Total formula weight: 57335.83

Authors

Vu, H.H.,Chang, J.H. (deposition date: 2021-02-22, release date: 2021-04-14, Last modification date: 2023-11-29)

Primary citation

Vu, H.H.,Jin, C.,Chang, J.H.
Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis.
Biochem.Biophys.Res.Commun., 553:85-91, 2021

PubMed Abstract: Glucose-6-phosphate dehydrogenase is the first enzyme in the pentose phosphate pathway. The reaction catalyzed by the enzyme is considered to be the main source of reducing power for nicotinamide adenine dinucleotide phosphate (NADPH) and is a precursor of 5-carbon sugar used by cells. To uncover the structural features of the enzyme, we determined the crystal structures of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis (KlG6PD) in both the apo form and a binary complex with its substrate glucose-6-phosphate. KlG6PD contains a Rossman-like domain for cofactor NADPH binding; it also presents a typical antiparallel β sheet at the C-terminal domain with relatively the same pattern as those of other homologous structures. Moreover, our structural and biochemical analyses revealed that Lys153 contributes significantly to substrate G6P recognition. This study may provide insights into the structural variation and catalytic features of the G6PD enzyme.

PubMed: 33765558
DOI: 10.1016/j.bbrc.2021.02.088

Experimental method

X-RAY DIFFRACTION (2.39 Å)