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Structure paper

TitleContribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Journal, issue, pagesProtein Eng., Vol. 9, Page 69-75, Year 1996
Publish dateDec 5, 1995 (structure data deposition date)
AuthorsFiner-Moore, J.S. / Fauman, E.B. / Morse, R.J. / Santi, D.V. / Stroud, R.M.
External linksProtein Eng. / PubMed:9053905
MethodsX-ray diffraction
Resolution2.2 - 2.9 Å
Structure data

PDB-1tsv:
THYMIDYLATE SYNTHASE R179A MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-1tsw:
THYMIDYLATE SYNTHASE R179A MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1tsx:
THYMIDYLATE SYNTHASE R179E MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1tsy:
THYMIDYLATE SYNTHASE R179K MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1tsz:
THYMIDYLATE SYNTHASE R179K MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-UMP:
2'-DEOXYURIDINE 5'-MONOPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • lactobacillus casei (bacteria)
KeywordsTRANSFERASE / METHYLTRANSFERASE / NUCLEOTIDE BIOSYNTHESIS

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