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TitleAllosteric role of a structural NADP molecule in glucose-6-phosphate dehydrogenase activity.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 29, Page e2119695119, Year 2022
Publish dateJul 19, 2022
AuthorsXuepeng Wei / Kathryn Kixmoeller / Elana Baltrusaitis / Xiaolu Yang / Ronen Marmorstein /
PubMed AbstractHuman 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 ...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. G6PD is a multimeric enzyme that uses the cofactors β-D-glucose 6-phosphate (G6P) and "catalytic" NADP (NADPc), as well as a "structural" NADP (NADPs) located ∼25 Å from the active site, to generate NADPH. While X-ray crystallographic and biochemical studies have revealed a role for NADPs in maintaining the catalytic activity by stabilizing the multimeric G6PD conformation, other potential roles for NADPs have not been evaluated. Here, we determined the high resolution cryo-electron microscopy structures of human wild-type G6PD in the absence of bound ligands and a catalytic G6PD-D200N mutant bound to NADPc and NADPs in the absence or presence of G6P. A comparison of these structures, together with previously reported structures, reveals that the unliganded human G6PD forms a mixture of dimers and tetramers with similar overall folds, and binding of NADPs induces a structural ordering of a C-terminal extension region and allosterically regulates G6P binding and catalysis. These studies have implications for understanding G6PD deficiencies and for therapy of G6PD-mediated disorders.
External linksProc Natl Acad Sci U S A / PubMed:35858355 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 3.7 Å
Structure data

EMDB-25224, PDB-7snf:
Structure of G6PD-WT dimer
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-25225, PDB-7sng:
structure of G6PD-WT tetramer
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-25226, PDB-7snh:
Structure of G6PD-D200N tetramer bound to NADP+
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-25227, PDB-7sni:
Structure of G6PD-D200N tetramer bound to NADP+ and G6P
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-26030, PDB-7toe:
Structure of G6PD-WT tetramer with no symmetry imposed
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-26031, PDB-7tof:
Structure of G6PD-WT dimer with no symmetry applied
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-26428, PDB-7ual:
Structure of G6PD-D200N tetramer bound to NADP+ and G6P with no symmetry applied
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-26442, PDB-7uc2:
Structure of G6PD-D200N tetramer bound to NADP+ with no symmetry applied
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-BG6:
6-O-phosphono-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / dehydrogenase / apo protein / D200N mutant / Glucose-6-phosphate 1-dehydrogenase

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