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TitleThe structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 20404-20410, Year 2019
Publish dateJul 27, 2019 (structure data deposition date)
AuthorsFernandez, A.J. / Daniel, E.J.P. / Mahajan, S.P. / Gray, J.J. / Gerken, T.A. / Tabak, L.A. / Samara, N.L.
External linksProc. Natl. Acad. Sci. USA / PubMed:31548401
MethodsX-ray diffraction
Resolution2.007 Å
Structure data

PDB-6pxu:
Crystal structure of human GalNAc-T12 bound to a diglycosylated peptide, Mn2+, and UDP
Method: X-RAY DIFFRACTION / Resolution: 2.007 Å

Chemicals

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

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-MN:
Unknown entry

ChemComp-A2G:
2-acetamido-2-deoxy-alpha-D-galactopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsTRANSFERASE / GalNAc-T / mucin-type O-glycosylation / enzyme catalysis / substrate selectivity / colorectal cancer / CRC

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