PDBsum entry 7e6h

Oxidoreductase

PDB id: 7e6h

Contents

Protein chain

484 a.a.

Ligands

TRS

7PE

Waters ×61

PDB id:

7e6h

Name:

Oxidoreductase

Title:

Glucose-6-phosphate dehydrogenase from kluyveromyces lactis

Structure:

Glucose-6-phosphate 1-dehydrogenase. Chain: a. Synonym: g6pd. Engineered: yes

Source:

Kluyveromyces lactis (strain atcc 8585 / cbs 2359 / dsm 70799 / nbrc 1267 / nrrl y-1140 / wm37). Yeast. Organism_taxid: 284590. Strain: atcc 8585 / cbs 2359 / dsm 70799 / nbrc 1267 / nrrl y-1140 / wm37. Gene: zwf, klla0d19855g. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.70Å R-factor: 0.191 R-free: 0.237

Authors:

V.H.Ha,J.H.Chang

Key ref:

H.H.Vu et al. (2021). Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis. Biochem Biophys Res Commun, 553, 85-91. PubMed id: 33765558 DOI: 10.1016/j.bbrc.2021.02.088

Date:

22-Feb-21 Release date: 14-Apr-21

Protein chain

P48828  (G6PD_KLULA) -  Glucose-6-phosphate 1-dehydrogenase from Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)

Seq: 497 a.a.

Struc: 484 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.49 - glucose-6-phosphate dehydrogenase (NADP(+)).
• Pathway: Pentose Phosphate Pathway (early stages)
• Reaction: D-glucose 6-phosphate + NADP⁺ = 6-phospho-D-glucono-1,5-lactone + NADPH + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.bbrc.2021.02.088

Biochem Biophys Res Commun 553:85-91 (2021)

PubMed id: 33765558

Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis.

H.H.Vu, C.Jin, J.H.Chang.

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.