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Structure paper

TitleActive-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 132, Page 438-439, Year 2010
Publish dateJul 13, 2009 (structure data deposition date)
AuthorsBrandt, G.S. / Kneen, M.M. / Petsko, G.A. / Ringe, D. / McLeish, M.J.
External linksJ. Am. Chem. Soc. / PubMed:20030408
MethodsX-ray diffraction
Resolution2.3 - 2.8 Å
Structure data

PDB-3iae:
Structure of benzaldehyde lyase A28S mutant with benzoylphosphonate
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3iaf:
Structure of benzaldehyde lyase A28S mutant with monomethyl benzoylphosphonate
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-D7K:
3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • pseudomonas fluorescens (bacteria)
KeywordsLYASE / thiamine adduct / phosphoserine / covalent sidechain adduct

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