5BPG

Crystal structure of the water-soluble FraC purified starting from the trans-membrane pore

Summary for 5BPG

• Entry DOI: 10.2210/pdb5bpg/pdb
• Descriptor: Fragaceatoxin C, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: actinoporin, pore-forming toxin, membrane lipids, lipid-protein interaction, protein folding, detergent, protein-detergent interaction, toxin
• Biological source: Actinia fragacea (Strawberry anemone)
• Total number of polymer chains: 4
• Total formula weight: 80034.45

Authors

Caaveiro, J.M.M.,Tanaka, K.,Tsumoto, K. (deposition date: 2015-05-28, release date: 2015-11-18, Last modification date: 2023-11-08)

Primary citation

Tanaka, K.,Caaveiro, J.M.,Tsumoto, K.
Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States
Biochemistry, 54:6863-6866, 2015

PubMed Abstract: The bidirectional transformation of a protein between its native water-soluble and integral transmembrane conformations is demonstrated for FraC, a hemolytic protein of the family of pore-forming toxins. In the presence of biological membranes, the water-soluble conformation of FraC undergoes a remarkable structural reorganization generating cytolytic transmembrane nanopores conducive to cell death. So far, the reverse transformation from the native transmembrane conformation to the native water-soluble conformation has not been reported. We describe the use of detergents with different physicochemical properties to achieve the spontaneous conversion of transmembrane pores of FraC back into the initial water-soluble state. Thermodynamic and kinetic stability data suggest that specific detergents cause an asymmetric change in the energy landscape of the protein, allowing the bidirectional transformation of a membrane protein.

PubMed: 26544760
DOI: 10.1021/acs.biochem.5b01112

Experimental method

X-RAY DIFFRACTION (2.14 Å)