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Structure paper

TitleStructural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.
Journal, issue, pagesJ. Mol. Biol., Vol. 281, Page 285-299, Year 1998
Publish dateNov 24, 1997 (structure data deposition date)
AuthorsPugmire, M.J. / Cook, W.J. / Jasanoff, A. / Walter, M.R. / Ealick, S.E.
External linksJ. Mol. Biol. / PubMed:9698549
MethodsX-ray diffraction
Resolution2.6 - 3 Å
Structure data

PDB-1azy:
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-1otp:
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-2tpt:
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli (E. coli)
KeywordsGLYCOSYLTRANSFERASE / THYMIDINE PHOSPHORYLASE / SALVAGE PATHWAY / PHOSPHORYLASE / PYRIMIDINE METABOLISM / DOMAIN MOVEMENT / TRANSFERASE

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