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TitleThe role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2'-deoxyuridine 5'-monophosphate (dUMP)-binding Tyr-261
Journal, issue, pagesBiochemistry, Vol. 45, Page 7415-7428, Year 2006
Publish dateMar 1, 2006 (structure data deposition date)
AuthorsNewby, Z. / Lee, T.T. / Morse, R.J. / Liu, Y. / Liu, L. / Venkatraman, P. / Santi, D.V. / Finer-Moore, J.S. / Stroud, R.M.
External linksBiochemistry / PubMed:16768437
MethodsX-ray diffraction
Resolution2.4 - 2.5 Å
Structure data

PDB-2g86:
L. casei thymidylate synthase Y261F in complex with substrate, dUMP
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2g89:
L. casei thymidylate synthase Y261A in complex with substrate, dUMP
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-2g8a:
Lactobacillus casei Y261M in complex with substrate, dUMP
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2g8d:
Lactobacillus casei thymidylate synthase Y261W-dUMP complex
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • lactobacillus casei (bacteria)
KeywordsTRANSFERASE / dUMP-binding residue / dUMP complex / thymidylate synthase mutant / alpha/beta protein / beta sheet / active site mutation / alpha-beta protein / methyltransferase

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