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Structure paper

TitleThe mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 28514-28523, Year 2013
Publish dateSep 5, 2012 (structure data deposition date)
AuthorsWeber, B.W. / Kimani, S.W. / Varsani, A. / Cowan, D.A. / Hunter, R. / Venter, G.A. / Gumbart, J.C. / Sewell, B.T.
External linksJ. Biol. Chem. / PubMed:23946488
MethodsX-ray diffraction
Resolution1.1 - 1.9 Å
Structure data

PDB-4gyl:
The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4gyn:
The E142L mutant of the amidase from Geobacillus pallidus
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4kzf:
The mechanism of the amidases: The effect of the mutation E142L in the amidase from Geobacillus pallidus
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4lf0:
The E142D mutant of the amidase from Geobacillus pallidus
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-ROP:
PROPIONAMIDE

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bacillus sp. (bacteria)
KeywordsHYDROLASE / amidase / catalytic tetrad / amidase mechanism / acrylamide / Michael Adduct / active site / chloride ion / cysteine 166 oxidation / alpha-beta-beta-alpha sandwich

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