1o72: Difference between revisions

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.

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].  

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