1o72
|
CRYSTAL STRUCTURE OF THE WATER-SOLUBLE STATE OF THE PORE-FORMING CYTOLYSIN STICHOLYSIN II COMPLEXED WITH PHOSPHORYLCHOLINE
OverviewOverview
Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea, anemone Stichodactyla helianthus. We found out that StnII exists in a, monomeric soluble state but forms tetramers in the presence of a lipidic, interface. Both structures have been independently determined at 1.7 A and, 18 A resolution, respectively, by using X-ray crystallography and electron, microscopy of two-dimensional crystals. Besides, the structure of soluble, StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a, region with an unusually high abundance of aromatic residues. Fitting of, the atomic model into the electron microscopy density envelope suggests, that while the beta sandwich structure of the protein remains ... [(full description)]
About this StructureAbout this Structure
1O72 is a [Single protein] structure of sequence from [Stichodactyla helianthus] with PC as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation., Mancheno JM, Martin-Benito J, Martinez-Ripoll M, Gavilanes JG, Hermoso JA, Structure. 2003 Nov;11(11):1319-28. PMID:14604522
Page seeded by OCA on Mon Oct 29 21:31:13 2007