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Structure paper

TitleGlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 25, Page 217-224, Year 2018
Publish dateDec 14, 2017 (structure data deposition date)
AuthorsYoo, J. / Mashalidis, E.H. / Kuk, A.C.Y. / Yamamoto, K. / Kaeser, B. / Ichikawa, S. / Lee, S.Y.
External linksNat. Struct. Mol. Biol. / PubMed:29459785
MethodsX-ray diffraction
Resolution2.95 - 3.1 Å
Structure data

PDB-6bw5:
Human GPT (DPAGT1) in complex with tunicamycin
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6bw6:
Human GPT (DPAGT1) H129 variant in complex with tunicamycin
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-TUM:
Tunicamycin / antibiotic*YM

ChemComp-PGW:
(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE/ANTIBIOTIC / N-linked glycosylation / endoplasmic reticulum / tunicamycin / natural product / TRANSFERASE / TRANSFERASE-ANTIBIOTIC complex

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