1o72: Difference between revisions
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==Overview== | ==Overview== | ||
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 .. | 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 Structure== | ==About this Structure== | ||
1O72 is a | 1O72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus] with PC as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O72 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: pore-forming toxin]] | [[Category: pore-forming toxin]] | ||
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Revision as of 16:06, 5 November 2007
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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 with PC as ligand. Structure known Active Site: AC1. 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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