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TitleEnergetic contributions of four arginines to phosphate-binding in thymidylate synthase are more than additive and depend on optimization of "effective charge balance".
Journal, issue, pagesBiochemistry, Vol. 39, Page 1011-1020, Year 2000
Publish dateAug 10, 1998 (structure data deposition date)
AuthorsMorse, R.J. / Kawase, S. / Santi, D.V. / Finer-Moore, J. / Stroud, R.M.
External linksBiochemistry / PubMed:10653645
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-1bo7:
THYMIDYLATE SYNTHASE R179T MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1bo8:
THYMIDYLATE SYNTHASE R178T MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1bp0:
THYMIDYLATE SYNTHASE R23I MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1bp6:
THYMIDYLATE SYNTHASE R23I, R179T DOUBLE MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1bpj:
THYMIDYLATE SYNTHASE R178T, R179T DOUBLE MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-U5P:
URIDINE-5'-MONOPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

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

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

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