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Structure paper

TitleStructural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases d
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 13658-13664, Year 2005
Publish dateNov 3, 2004 (structure data deposition date)
AuthorsMurakami, M.T. / Gabdoulkhakov, A. / Fernandes-Pedrosa, M.F. / Tambourgi, D.V. / Arni, R.K.
External linksJ. Biol. Chem. / PubMed:15654080
MethodsX-ray diffraction
Resolution1.75 - 1.85 Å
Structure data

PDB-1xx1:
Structural basis for ion-coordination and the catalytic mechanism of sphingomyelinases D
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-2f9r:
Crystal structure of the inactive state of the Smase I, a sphingomyelinase D from Loxosceles laeta venom
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-MG:
Unknown entry

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • loxosceles laeta (spider)
KeywordsHYDROLASE / quick cryo-soaking / activity / SMase D / sphingomyelinase D / catalytic activity / magnesium-binding site / inactive state

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