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Structure paper

TitleStructure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable PI-Cation Latched Loop
Journal, issue, pagesBiochemistry, Vol. 51, Page 2579-2587, Year 2012
Publish dateDec 9, 2011 (structure data deposition date)
AuthorsGoldstein, R. / Cheng, J. / Stec, B. / Roberts, M.F.
External linksBiochemistry / PubMed:22390775
MethodsX-ray diffraction
Resolution1.9 - 2.34 Å
Structure data

PDB-3v16:
An intramolecular pi-cation latch in phosphatidylinositol-specific phospholipase C from S.aureus controls substrate access to the active site
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3v18:
Structure of the Phosphatidylinositol-specific phospholipase C from Staphylococcus aureus
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

PDB-3v1h:
Structure of the H258Y mutant of Phosphatidylinositol-specific phospholipase C from Staphylococcus aureus
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

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

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-ACT:
ACETATE ION

Source
  • staphylococcus aureus subsp. aureus (bacteria)
KeywordsLYASE / pi-cation / TIM barrel / phospholipase

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