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Structure paper

TitleStructure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.
Journal, issue, pagesNat. Struct. Biol., Vol. 4, Page 601-604, Year 1997
Publish dateJun 12, 1997 (structure data deposition date)
AuthorsLavie, A. / Vetter, I.R. / Konrad, M. / Goody, R.S. / Reinstein, J. / Schlichting, I.
External linksNat. Struct. Biol. / PubMed:9253404
MethodsX-ray diffraction
Resolution2.1 - 2.4 Å
Structure data

PDB-1tmk:
YEAST THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (DTMP)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2tmk:
YEAST THYMIDYLATE KINASE COMPLEXED WITH 3'-AZIDO-3'-DEOXYTHYMIDINE MONOPHOSPHATE (AZT-MP)
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-TMP:
THYMIDINE-5'-PHOSPHATE

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ATM:
3'-AZIDO-3'-DEOXYTHYMIDINE-5'-MONOPHOSPHATE

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPHOSPHOTRANSFERASE / TRANSFERASE (PHOSPHOTRANSFERASE) / KINASE / THYMIDINE ACTIVATION PATHWAY / ENZYME / AZT

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