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TitleCryo-EM structure and regulation of human NAD kinase.
Journal, issue, pagesSci Adv, Vol. 11, Issue 4, Page eads2664, Year 2025
Publish dateJan 24, 2025
AuthorsPrakash P Praharaj / Yang Li / Charline Mary / Mona H Soflaee / Kevin Ryu / Dohun Kim / Diem H Tran / Trishna Dey / Harrison J Tom / Halie Rion / Muriel Gelin / Andrew Lemoff / Lauren G Zacharias / João S Patricio / Thomas P Mathews / Zhe Chen / Corinne Lionne / Gerta Hoxhaj / Gilles Labesse /
PubMed AbstractReduced nicotinamide adenine dinucleotide phosphate (NADPH) is a crucial reducing cofactor for reductive biosynthesis and protection from oxidative stress. To fulfill their heightened anabolic and ...Reduced nicotinamide adenine dinucleotide phosphate (NADPH) is a crucial reducing cofactor for reductive biosynthesis and protection from oxidative stress. To fulfill their heightened anabolic and reductive power demands, cancer cells must boost their NADPH production. Progrowth and mitogenic protein kinases promote the activity of cytosolic NAD kinase (NADK), which produces NADP, a limiting NADPH precursor. However, the molecular architecture and mechanistic regulation of human NADK remain undescribed. Here, we report the cryo-electron microscopy structure of human NADK, both in its apo-form and in complex with its substrate NAD (nicotinamide adenine dinucleotide), revealing a tetrameric organization with distinct structural features. We discover that the amino (N)- and carboxyl (C)-terminal tails of NADK have opposing effects on its enzymatic activity and cellular NADP(H) levels. Specifically, the C-terminal region is critical for NADK activity, whereas the N-terminal region exhibits an inhibitory role. This study highlights molecular insights into the regulation of a vital enzyme governing NADP(H) production.
External linksSci Adv / PubMed:39854463 / PubMed Central
MethodsEM (single particle)
Resolution2.34 - 3.18 Å
Structure data

45831

9cr3

EMDB-45831, PDB-9cr3:
CryoEM Structure of the human full length NAD Kinase
Method: EM (single particle) / Resolution: 3.18 Å

45832

9cr4

EMDB-45832, PDB-9cr4:
CryoEM Structure of the C-terminally truncated form of human NAD Kinase
Method: EM (single particle) / Resolution: 2.81 Å

45856

9cra

EMDB-45856, PDB-9cra:
CryoEM Structure of the C-terminally truncated form of human NAD Kinase bound to NAD
Method: EM (single particle) / Resolution: 2.34 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / catalyzes the reaction of ATP + NAD+ = ADP + H+ + NADP+

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