Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea

Koldo Morante, Jose M.M. Caaveiro, Ana Rosa Viguera, Kouhei Tsumoto, Juan Manuel González-Mañas

Research output: Contribution to journalArticle

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Abstract

Actinoporins are pore-forming toxins produced by different sea anemones that self-assemble within the membranes of their target cells and compromise their function as a permeability barrier. The recently published three-dimensional structures of two oligomeric complexes formed by fragaceatoxin C point to Val60 as a key residue involved in the oligomerization of the functional pore.
To gain insight into the mechanism of toxin oligomerization, different point mutations have been introduced at this position. Functional characterization of the muteins suggests that Val60 represents a hot-spot where the introduction of mutations hinders protein assembly and reduces the overall affinity for membranes.
Original languageEnglish
Pages (from-to)1840-1846
Number of pages7
JournalFEBS Letters
Volume589
DOIs
Publication statusPublished - 2015

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Actinium
Oligomerization
Sea Anemones
Membranes
Point Mutation
Permeability
Mutation
Proteins
fragaceatoxin C

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Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea. / Morante, Koldo; Caaveiro, Jose M.M.; Viguera, Ana Rosa; Tsumoto, Kouhei; González-Mañas, Juan Manuel.

In: FEBS Letters, Vol. 589, 2015, p. 1840-1846.

Research output: Contribution to journalArticle

Morante, Koldo ; Caaveiro, Jose M.M. ; Viguera, Ana Rosa ; Tsumoto, Kouhei ; González-Mañas, Juan Manuel. / Functional characterization of Val60, a key residue involved in the membrane-oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea. In: FEBS Letters. 2015 ; Vol. 589. pp. 1840-1846.
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AU - Tsumoto, Kouhei

AU - González-Mañas, Juan Manuel

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AB - Actinoporins are pore-forming toxins produced by different sea anemones that self-assemble within the membranes of their target cells and compromise their function as a permeability barrier. The recently published three-dimensional structures of two oligomeric complexes formed by fragaceatoxin C point to Val60 as a key residue involved in the oligomerization of the functional pore.To gain insight into the mechanism of toxin oligomerization, different point mutations have been introduced at this position. Functional characterization of the muteins suggests that Val60 represents a hot-spot where the introduction of mutations hinders protein assembly and reduces the overall affinity for membranes.

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