Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin |
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Authors: | Narayan Kartik Chumnarnsilpa Sakesit Choe Han Irobi Edward Urosev Dunja Lindberg Uno Schutt Clarence E Burtnick Leslie D Robinson Robert C |
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Institution: | Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, 751 23 Uppsala, Sweden. |
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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 A 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. |
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