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Structure paper

TitleStructural basis of protein arginine rhamnosylation by glycosyltransferase EarP
Journal, issue, pagesNat. Chem. Biol., Vol. 14, Page 368-374, Year 2018
Publish dateJan 7, 2017 (structure data deposition date)
AuthorsSengoku, T. / Suzuki, T. / Dohmae, N. / Watanabe, C. / Honma, T. / Hikida, Y. / Yamaguchi, Y. / Takahashi, H. / Yokoyama, S. / Yanagisawa, T.
External linksNat. Chem. Biol. / PubMed:29440735
MethodsX-ray diffraction
Resolution1.63 - 2 Å
Structure data

PDB-5wxi:
EarP bound with dTDP-rhamnose (soaked)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5wxj:
Apo EarP
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5wxk:
EarP bound with domain I of EF-P
Method: X-RAY DIFFRACTION / Resolution: 1.801 Å

PDB-5xvr:
EarP bound with dTDP-rhamnose (co-crystal)
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-TRH:
2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-TYD:
THYMIDINE-5'-DIPHOSPHATE

ChemComp-NI:
NICKEL (II) ION

Source
  • neisseria meningitidis serogroup b / serotype 15 (strain h44/76) (bacteria)
  • neisseria meningitidis h44/76 (bacteria)
KeywordsTRANSFERASE / glycosyltransferase / GT-B / EF-P / rhamnosylation / translation elongation / dTDP-rhamnose

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