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Activation in isolation: exposure of the actin‐binding site in the C‐terminal half of gelsolin does not require actin 1
Author(s) -
Narayan Kartik,
Chumnarnsilpa Sakesit,
Choe Han,
Irobi Edward,
Urosev Dunja,
Lindberg Uno,
Schutt Clarence E.,
Burtnick Leslie D.,
Robinson Robert C.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00933-5
Subject(s) - gelsolin , actin , chemistry , actina , binding site , biophysics , actin binding protein , biochemistry , actin cytoskeleton , biology , cytoskeleton , cell
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 Å resolution in the presence of Ca 2+ 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 Ca 2+ sites occupied. Neither actin nor the type‐l Ca 2+ , which normally is sandwiched between actin and G4, is required to achieve this conformation.