1O71

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

1O71 の概要

• エントリーDOI: 10.2210/pdb1o71/pdb
• 関連するPDBエントリー: 1GWY 1O72
• 分子名称: STICHOLYSIN II, GLYCEROL (3 entities in total)
• 機能のキーワード: cytolysin, pore-forming toxin, membrane interaction, hemolysis
• 由来する生物種: STOICHACTIS HELIANTHUS (CARRIBEAN SEA ANEMONE)
• 細胞内の位置: Secreted: P07845
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39158.25

構造登録者

Mancheno, J.M.,Martinez-Ripoll, M.,Gavilanes, J.G.,Hermoso, J.A. (登録日: 2002-10-23, 公開日: 2003-11-13, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.26 Å)