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TitleStructure Determination and Biochemical Studies on Bacillus Stearothermophilus E53Q Serine Hydroxymethyltransferase and its Complexes Provide Insights on Function and Enzyme Memory
Journal, issue, pagesFEBS J., Vol. 274, Page 4148-, Year 2007
Publish dateNov 15, 2007 (structure data deposition date)
AuthorsRajaram, V. / Bhavani, B.S. / Kaul, P. / Prakash, V. / Appaji Rao, N. / Savithri, H.S. / Murthy, M.R.N.
External linksFEBS J. / PubMed:17651438
MethodsX-ray diffraction
Resolution1.8 - 2.3 Å
Structure data

PDB-2vgs:
Crystal structure of E53QbsSHMT internal aldimine
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2vgt:
Crystal structure of E53QbsSHMT with glycine
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-2vgu:
Crystal structure of E53QbsSHMT with L-serine
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2vgv:
Crystal structure of E53QbsSHMT obtained in the presence of L-allo- Threonine
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2vgw:
Crystal structure of E53QbsSHMT obtained in the presence of glycine and 5-fomyl tetrahydrofolate
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

ChemComp-PO4:
PHOSPHATE ION

ChemComp-SER:
SERINE

Source
  • bacillus stearothermophilus (bacteria)
KeywordsTRANSFERASE / PLP-DEPENDENT ENZYMES / SERINE HYDROXYMETHYLTRANSFERASE / SHMT / E53Q / ENZYME MEMORY / PYRIDOXAL PHOSPHATE / ONE-CARBON METABOLISM / FTHF

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