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TitleModulation of bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 15607-15618, Year 2009
Publish dateAug 24, 2008 (structure data deposition date)
AuthorsShi, X. / Shao, C. / Zhang, X. / Zambonelli, C. / Redfield, A.G. / Head, J.F. / Seaton, B.A. / Roberts, M.F.
External linksJ. Biol. Chem. / PubMed:19369255
MethodsX-ray diffraction
Resolution1.75 - 1.95 Å
Structure data

PDB-3ea1:
Crystal Structure of the Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-3ea2:
Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3ea3:
Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-INS:
1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE

ChemComp-MN:
Unknown entry

Source
  • bacillus thuringiensis (bacteria)
KeywordsLYASE / phosphatidylinositol-specific phospholipase C / PI-PLC / Dimer / interfacially impaired / membrane binding / TIM barrel / Lipid degradation / Secreted / myo-inositol

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