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TitleCryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 6952, Year 2023
Publish dateOct 31, 2023
AuthorsPing Lu / Yusong Liu / Maozhou He / Ting Cao / Mengquan Yang / Shutao Qi / Hongtao Yu / Haishan Gao /
PubMed AbstractO-GlcNAcylation is a conserved post-translational modification that attaches N-acetyl glucosamine (GlcNAc) to myriad cellular proteins. In response to nutritional and hormonal signals, O- ...O-GlcNAcylation is a conserved post-translational modification that attaches N-acetyl glucosamine (GlcNAc) to myriad cellular proteins. In response to nutritional and hormonal signals, O-GlcNAcylation regulates diverse cellular processes by modulating the stability, structure, and function of target proteins. Dysregulation of O-GlcNAcylation has been implicated in the pathogenesis of cancer, diabetes, and neurodegeneration. A single pair of enzymes, the O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), catalyzes the addition and removal of O-GlcNAc on over 3,000 proteins in the human proteome. However, how OGT selects its native substrates and maintains the homeostatic control of O-GlcNAcylation of so many substrates against OGA is not fully understood. Here, we present the cryo-electron microscopy (cryo-EM) structures of human OGT and the OGT-OGA complex. Our studies reveal that OGT forms a functionally important scissor-shaped dimer. Within the OGT-OGA complex structure, a long flexible OGA segment occupies the extended substrate-binding groove of OGT and positions a serine for O-GlcNAcylation, thus preventing OGT from modifying other substrates. Conversely, OGT disrupts the functional dimerization of OGA and occludes its active site, resulting in the blocking of access by other substrates. This mutual inhibition between OGT and OGA may limit the futile O-GlcNAcylation cycles and help to maintain O-GlcNAc homeostasis.
External linksNat Commun / PubMed:37907462 / PubMed Central
MethodsEM (single particle)
Resolution3.82 - 5.86 Å
Structure data

EMDB-33767: Human OGT-OGA complex (conformation I)
Method: EM (single particle) / Resolution: 5.68 Å

33768

7yea

EMDB-33768, PDB-7yea:
Human O-GlcNAc transferase Dimer
Method: EM (single particle) / Resolution: 3.82 Å

EMDB-33769: Human OGT-OGA complex (Conformation III)
Method: EM (single particle) / Resolution: 5.86 Å

33773

7yeh

EMDB-33773, PDB-7yeh:
Cryo-EM structure of human OGT-OGA complex
Method: EM (single particle) / Resolution: 3.92 Å

Chemicals

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Human O-GlcNAc transferase Dimer / TRANSFERASE/HYDROLASE / O-GlcNAc transferase / O-GlcNAcase / Complex / Mutual inhibition / TRANSFERASE-HYDROLASE complex

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