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Structure paper

TitleStructures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.
Journal, issue, pagesCell, Vol. 175, Page 1045-1058.e16, Year 2018
Publish dateJun 30, 2016 (structure data deposition date)
AuthorsDong, Y.Y. / Wang, H. / Pike, A.C.W. / Cochrane, S.A. / Hamedzadeh, S. / Wyszynski, F.J. / Bushell, S.R. / Royer, S.F. / Widdick, D.A. / Sajid, A. ...Dong, Y.Y. / Wang, H. / Pike, A.C.W. / Cochrane, S.A. / Hamedzadeh, S. / Wyszynski, F.J. / Bushell, S.R. / Royer, S.F. / Widdick, D.A. / Sajid, A. / Boshoff, H.I. / Park, Y. / Lucas, R. / Liu, W.M. / Lee, S.S. / Machida, T. / Minall, L. / Mehmood, S. / Belaya, K. / Liu, W.W. / Chu, A. / Shrestha, L. / Mukhopadhyay, S.M.M. / Strain-Damerell, C. / Chalk, R. / Burgess-Brown, N.A. / Bibb, M.J. / Barry Iii, C.E. / Robinson, C.V. / Beeson, D. / Davis, B.G. / Carpenter, E.P.
External linksCell / PubMed:30388443
MethodsX-ray diffraction
Resolution3.1 - 3.6 Å
Structure data

PDB-5lev:
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant)
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-5o5e:
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) in complex with tunicamycin
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-6fm9:
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1)
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-6fwz:
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) in complex with UDP-GlcNAc
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-HOH:
WATER

ChemComp-P6L:
(2S)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(6E)-HEXADEC-6-ENOYLOXY]PROPYL (8E)-OCTADEC-8-ENOATE / phospholipid*YM

ChemComp-9LH:
Tunicamycin / antibiotic*YM

ChemComp-MG:
Unknown entry

ChemComp-UD1:
URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Protein glycosylation / integral membrane protein / congenital myasthenic syndrome 13 / Structural Genomics / Structural Genomics Consortium / SGC / PNPT / congenital myasthenic syndrome / antibiotic

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