|Title||Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin|
|Publication Type||Journal Article|
|Year of Publication||2003|
|Authors||Narayan, K, Chumnarnsilpa, S, Choe, H, Irobi, E, Urosev, D, Lindberg, U, Schutt, CE, Burtnick, LD, Robinson, RC|
|Type of Article||Article|
|Keywords||actin, calcium-activation, COMPLEX, DOMAINS, F-ACTIN, gelsolin, PLASMA GELSOLIN, REGULATORY PROTEIN, TRANSFORMATION|
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.
|URL||<Go to ISI>://000185583000002|