Mar 1, 2000 · Here, we present the first crystal structure of human G6PD, that of G6PD Canton R459L, and discuss its implications for the molecular basis of G6PD deficiency.

The crystal structure of G6PD reveals an extensive network of electrostatic interactions and hydrogen bonding involving G6P, 3 water molecules, 3 lysines, 1 arginine, 2 histidines, 2 glutamic acids, and other polar amino acids.

Crystallographic structure of the human wild-type (WT) G6PD enzyme (PDB entries 2BHL and 2BH9), showing the structural NADP + (blue molecular surface), catalytic NADP + (dark purple molecular surface), and G6P substrate (yellow molecular surface) in the dimer.

Jul 6, 2018 · As no medications are available to treat G6PD deficiency, here we seek to identify a small molecule that corrects it. Crystallographic study and mutagenesis analysis identify the structural and functional defect of one common mutant (Canton, R459L).

Jun 1, 2022 · Understanding the molecular basis of G6PD deficiency is also essential to determine how mutations influence enzyme structure, stability, and activity. In characterizing 34 G6PD variants selected from Class I, II, and III, we reviewed and compared structural and molecular characterizations.

We have determined the three–dimensional structure of L. mesenteroides G6PD, which shows the dimer to be an extended molecule. The monomers have two domains; the smaller amino–terminal domain has the typical dinucleotide–binding fold and, in the dimer, the coenzyme–binding sites are positioned at the extremities of the molecule.

G6PD mutations leading to its deficiency result in the neonatal jaundice and acute hemolytic anemia in human. Herein, we demonstrate the molecular dynamics simulations of the wildtype G6PD and its three mutants to monitor the effect of mutations on dynamics and stability of …

Dec 17, 2019 · To resolve this, we performed integral structural characterization of five G6PD mutants, including four class I mutants, associated with the noncatalytic NADP + and dimerization, using crystallography, small-angle X-ray scattering (SAXS), cryogenic electron microscopy (cryo-EM), and biophysical analyses. Comparisons with the structure and ...

Results: The structure of G6PD has been determined and refined to 2.0 A resolution. The enzyme is a dimer, each subunit consisting of two domains. The smaller domain is a classic dinucleotide-binding fold, while the larger one is a new +ct fold, not previously seen, with a predominantly antiparallel nine-stranded -sheet. There.

Oct 28, 2021 · Human glucose-6-phosphate dehydrogenase (G6PD) is the main cellular source of NADPH, and thus plays a key role in maintaining reduced glutathione to protect cells from oxidative stress disorders such as hemolytic anemia.