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TitleStructure of a truncated human GlcNAc-1-phosphotransferase variant reveals the basis for its hyperactivity.
Journal, issue, pagesJ Biol Chem, Vol. 300, Issue 9, Page 107706, Year 2024
Publish dateAug 22, 2024
AuthorsHua Li / Balraj Doray / Benjamin C Jennings / Wang-Sik Lee / Lin Liu / Stuart Kornfeld / Huilin Li /
PubMed AbstractMutations that cause loss of function of GlcNAc-1-phosphotransferase (PTase) lead to the lysosomal storage disorder mucolipidosis II. PTase is the key enzyme of the mannose 6-phosphate (M6P) ...Mutations that cause loss of function of GlcNAc-1-phosphotransferase (PTase) lead to the lysosomal storage disorder mucolipidosis II. PTase is the key enzyme of the mannose 6-phosphate (M6P) targeting system that is responsible for tagging lysosomal hydrolases with the M6P moiety for their delivery to the lysosome. We had previously generated a truncated hyperactive form of PTase termed S1S3 which was shown to notably increase the phosphorylation level of secreted lysosomal enzymes and enhance their uptake by cells. Here, we report the 3.4 Å cryo-EM structure of soluble S1S3 lacking both transmembrane domains and cytosolic tails. The structure reveals a high degree of conservation of the catalytic core to full-length PTase. In this dimeric structure, the EF-hand of one protomer is observed interacting with the conserved region four of the other. In addition, we present a high-quality EM 3D map of the UDP-GlcNAc bound form of the full-length soluble protein showing the key molecular interactions between the nucleotide sugar donor and side chain amino acids of the protein. Finally, although the domain organization of S1S3 is very similar to that of the Drosophila melanogaster (fruit fly) PTase homolog, we establish that the latter does not act on lysosomal hydrolases.
External linksJ Biol Chem / PubMed:39178950 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.4 Å
Structure data

44511

9bgf

EMDB-44511, PDB-9bgf:
Structure of human GlcNAc-1-phosphotransferase complexed with the donor substrate UDP-GlcNAc
Method: EM (single particle) / Resolution: 2.9 Å

44512

9bgg

EMDB-44512, PDB-9bgg:
Structure of a hyperactive S1S3 truncation of the human GlcNAc-1-phosphotransferase
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-UD1:
URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE

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

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / GlcNAc-1-phosphotransferase / lysosomal hydrolases / mannose 6-phosphate trafficking pathway

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