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Structure paper

TitleCovalent modifications of the active site cysteine occur as a result of mutating the glutamate of the catalytic triad in the amidase from Nesterenkonia sp.
Journal, issue, pagesTo be Published
Publish dateJan 30, 2013 (structure data deposition date)
AuthorsKimani, S.W. / Hunter, R. / Vlok, M. / Watermeyer, J. / Sewell, B.T.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.4 - 1.92 Å
Structure data

PDB-4izs:
The C145A mutant of the amidase from Nesterenkonia sp. AN1 in complex with butyramide
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-4izt:
The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-4izu:
The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing the result of Michael addition of acrylamide at the active site cysteine
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-4izv:
The E41Q/C145A double mutant of the amidase from Nesterenkonia sp. AN1 in complex with acrylamide
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4izw:
The E41L mutant of the amidase from Nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-BMD:
BUTYRAMIDE

ChemComp-HOH:
WATER

ChemComp-ACM:
ACETAMIDE

ChemComp-FTM:
2-fluoroacetamide

ChemComp-ROP:
PROPIONAMIDE

ChemComp-1HC:
prop-2-enamide

Source
  • nesterenkonia sp. 10004 (bacteria)
KeywordsHYDROLASE / butyramide / hydrolase/substrate / fluoroacetamide / acetamide / hydrolase-substrate complex / propionamide / acrylamide (prop-2-enamide) / cysteine 145 / active site

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