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Structure paper

TitleRole of Lys-226 in the Catalytic Mechanism of Bacillus Stearothermophilus Serine Hydroxymethyltransferase-Crystal Structure and Kinetic Studies
Journal, issue, pagesBiochemistry, Vol. 44, Page 6929-6937, Year 2005
Publish dateJan 15, 2005 (structure data deposition date)
AuthorsBhavani, S. / Trivedi, V. / Jala, V.R. / Subramanya, H.S. / Kaul, P. / Purnima, K. / Prakash, V. / Appaji, R.N. / Savithri, H.S.
External linksBiochemistry / PubMed:15865438
MethodsX-ray diffraction
Resolution2 - 2.25 Å
Structure data

PDB-1yjs:
K226Q Mutant Of Serine Hydroxymethyltransferase From B. Stearothermophilus, Complex With Glycine
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1yjy:
K226M Mutant Of Serine Hydroxymethyltransferase From B. Stearothermophilus, Complex With Serine
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-1yjz:
K226M Mutant Of Serine Hydroxymethyltransferase From B. Stearothermophilus
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-GLY:
GLYCINE

ChemComp-HOH:
WATER

ChemComp-SER:
SERINE

Source
  • geobacillus stearothermophilus (bacteria)
KeywordsTRANSFERASE / SHMT / Mutant / Catalysis

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