1o72
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| , resolution 2.41Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 intact upon oligomerization, the N-terminal region and a flexible and highly basic loop undergo significant conformational changes. These results provide the structural basis for the membrane recognition step of actinoporins and unexpected insights into the oligomerization step.
About this StructureAbout this Structure
1O72 is a Single protein structure of sequence from Stichodactyla helianthus. 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
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