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TitleMechanism and linkage specificities of the dual retaining beta-Kdo glycosyltransferase modules of KpsC from bacterial capsule biosynthesis.
Journal, issue, pagesJ. Biol. Chem., Vol. 299, Page 104609-104609, Year 2023
Publish dateJan 18, 2023 (structure data deposition date)
AuthorsDoyle, L. / Ovchinnikova, O.G. / Huang, B.S. / Forrester, T.J.B. / Lowary, T.L. / Kimber, M.S. / Whitfield, C.
External linksJ. Biol. Chem. / PubMed:36924942
MethodsX-ray diffraction
Resolution1.2 - 1.9 Å
Structure data

PDB-8fuw:
KpsC D160N Kdo adduct
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-8fux:
KpsC D160C ternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-C5P:
CYTIDINE-5'-MONOPHOSPHATE

ChemComp-KDO:
3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-KD3:
3-deoxy-beta-D-manno-oct-2-ulopyranosonic acid

ChemComp-PXV:
N-(8-hydroxyoctyl)-4-methoxybenzamide

ChemComp-PO4:
PHOSPHATE ION

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / glycosyltransferase / retaining

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