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Structure paper

TitleStructures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins and its Mode of Sphingomyelin Recognition.
Journal, issue, pagesStructure, Vol. 20, Page 1498-, Year 2012
Publish dateAug 8, 2011 (structure data deposition date)
AuthorsDe Colibus, L. / Sonnen, A.F.P. / Morris, K.J. / Siebert, C.A. / Abrusci, P. / Plitzko, J. / Hodnik, V. / Leippe, M. / Volpi, E. / Anderluh, G. / Gilbert, R.J.C.
External linksStructure / PubMed:22819216
MethodsX-ray diffraction
Resolution2.84 - 3.3 Å
Structure data

PDB-3zx7:
Complex of lysenin with phosphocholine
Method: X-RAY DIFFRACTION / Resolution: 2.84 Å

PDB-3zxd:
wild-type lysenin
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

PDB-3zxg:
lysenin sphingomyelin complex
Method: X-RAY DIFFRACTION / Resolution: 3.12 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-PC:
PHOSPHOCHOLINE

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-0SM:
TRIMETHYL-[2-[[(2S,3S)-2-(OCTADECANOYLAMINO)-3-OXIDANYL-BUTOXY]-OXIDANYL-PHOSPHORYL]OXYETHYL]AZANIUM

Source
  • eisenia fetida (common brandling worm)
KeywordsTOXIN / PORE FORMING TOXIN / EARTHWORM / PORE-FORMING TOXIN

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