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Structure paper

TitleA 5000-fold increase in the specificity of a bacterial phosphotriesterase for malathion through combinatorial active site mutagenesis
Journal, issue, pagesPlos One, Vol. 9, Page e94177-e94177, Year 2014
Publish dateNov 21, 2013 (structure data deposition date)
AuthorsNaqvi, T. / Warden, A.C. / French, N. / Sugrue, E. / Carr, P.D. / Jackson, C.J. / Scott, C.
External linksPlos One / PubMed:24721933
MethodsX-ray diffraction
Resolution1.99 Å
Structure data

PDB-3wml:
Structure of phosphotriesterase mutant (S308L/Y309A) from Agrobacterium radiobacter
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-4np7:
Structure of phosphotriesterase mutant (S308L/Y309A) from Agrobacterium radiobacter with diethyl thiophosphate bound in the active site
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-FE2:
Unknown entry

ChemComp-CO:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-DPJ:
O,O-DIETHYL HYDROGEN THIOPHOSPHATE

Source
  • agrobacterium tumefaciens (bacteria)
KeywordsHYDROLASE / Phosphotriesterase

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