3ZWJ
CRYSTAL STRUCTURE OF THE PORE-FORMING TOXIN FRAC FROM ACTINIA FRAGACEA (Form 3)
Summary for 3ZWJ
| Entry DOI | 10.2210/pdb3zwj/pdb |
| Related | 3ZWG |
| Descriptor | FRAGACEATOXIN C (2 entities in total) |
| Functional Keywords | toxin, membrane proteins, pore-forming toxins, actinoporins |
| Biological source | ACTINIA FRAGACEA |
| Cellular location | Secreted (By similarity): B9W5G6 |
| Total number of polymer chains | 9 |
| Total formula weight | 177716.73 |
| Authors | Mechaly, A.E.,Bellomioa, A.,Morantea, K.,Gonzalez-Manas, J.M.,Guerin, D.M.A. (deposition date: 2011-08-01, release date: 2012-07-04, Last modification date: 2023-12-20) |
| Primary citation | Mechaly, A.E.,Bellomio, A.,Morante, K.,Agirre, J.,Gil-Carton, D.,Valle, M.,Gonzalez-Manas, J.M.,Guerin, D.M.A. Pores of the Toxin Frac Assemble Into 2D Hexagonal Clusters in Both Crystal Structures and Model Membranes. J.Struct.Biol., 180:312-, 2012 Cited by PubMed Abstract: The recent high-resolution structure of the toxin FraC derived from the sea anemone Actinia fragacea has provided new insight into the mechanism of pore formation by actinoporins. In this work, we report two new crystal forms of FraC in its oligomeric prepore conformation. Together with the previously reported structure, these two new structures reveal that ring-like nonamers of the toxin assemble into compact two-dimensional hexagonal arrays. This supramolecular organization is maintained in different relative orientations adopted by the oligomers within the crystal layers. Analyses of the aggregation of FraC pores in both planar and curved (vesicles) model membranes show similar 2D hexagonal arrangements. Our observations support a model in which hexagonal pore-packing is a clustering mechanism that maximizes toxin-driven membrane damage in the target cell. PubMed: 22728830DOI: 10.1016/J.JSB.2012.06.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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