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Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

TitleActivation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin
Publication TypeJournal Article
Year of Publication2003
AuthorsNarayan, K, Chumnarnsilpa, S, Choe, H, Irobi, E, Urosev, D, Lindberg, U, Schutt, CE, Burtnick, LD, Robinson, RC
JournalFebs Letters
Volume552
Pagination82-85
Date PublishedSep
Type of ArticleArticle
ISBN Number0014-5793
Keywordsactin, calcium-activation, COMPLEX, DOMAINS, F-ACTIN, gelsolin, PLASMA GELSOLIN, REGULATORY PROTEIN, TRANSFORMATION
Abstract

Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-1 Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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