1O71

Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II complexed with glycerol

Summary for 1O71

• Entry DOI: 10.2210/pdb1o71/pdb
• Related: 1GWY 1O72
• Descriptor: STICHOLYSIN II, GLYCEROL (3 entities in total)
• Functional Keywords: cytolysin, pore-forming toxin, membrane interaction, hemolysis
• Biological source: STOICHACTIS HELIANTHUS (CARRIBEAN SEA ANEMONE)
• Cellular location: Secreted: P07845
• Total number of polymer chains: 2
• Total formula weight: 39158.25

Authors

Mancheno, J.M.,Martinez-Ripoll, M.,Gavilanes, J.G.,Hermoso, J.A. (deposition date: 2002-10-23, release date: 2003-11-13, Last modification date: 2024-05-08)

Primary citation

Mancheno, J.M.,Martin-Benito, J.,Martinez-Ripoll, M.,Gavilanes, J.G.,Hermoso, J.A.
Crystal and Electron Microscopy Structures of Sticholysin II Actinoporin Reveal Insights Into the Mechanism of Membrane Pore Formation
Structure, 11:1319-, 2003

PubMed Abstract: 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.

PubMed: 14604522
DOI: 10.1016/J.STR.2003.09.019

Experimental method

X-RAY DIFFRACTION (2.26 Å)