Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function

García Linares, Sara; Castrillo, Inés; Bruix, Marta; Menéndez, Margarita; Alegre-Cebollada, Jorge; Martínez Del Pozo, Álvaro; Gavilanes Franco, José Gregorio

Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function

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Official URL

https://doi.org/10.1016/j.abb.2013.01.005

Publication date

2013

Authors

García Linares, Sara

Castrillo, Inés

Bruix, Marta

Menéndez, Margarita

Alegre-Cebollada, Jorge

Martínez Del Pozo, Álvaro

Gavilanes Franco, José Gregorio

Publisher

Elsevier

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URI

https://hdl.handle.net/20.500.14352/97736

Citation

García-Linares, Sara, et al. «Three-Dimensional Structure of the Actinoporin Sticholysin I. Influence of Long-Distance Effects on Protein Function». Archives of Biochemistry and Biophysics, vol. 532, n.o 1, abril de 2013, pp. 39-45. https://doi.org/10.1016/j.abb.2013.01.005

Abstract

Actinoporins are water-soluble proteins with the ability to form pores upon insertion into biological membranes. They constitute a family of proteins with high degree of sequence identities but different hemolytic activities, suggesting that minor conformational arrangements result in major functional changes. A good example of this situation is the sea anemone Stichodactyla helianthus which produces two very similar actinoporins, sticholysins I (StnI) and II (StnII), but of very different hemolytic efficiency. Within this idea, given that the high resolution three-dimensional structure of StnII is already known, we have now solved that one corresponding to StnI in order to analyze the influence of particular residues on the conformation and activity of these proteins. In addition, random mutagenesis has been also used to produce five less hemolytic variants of StnI. All these mutations map to functionally relevant regions because they are probably involved in conformational changes associated with pore formation, which take place after membrane binding, and involve long-distance rearrangements of the polypeptide chain of actinoporins.