Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin.
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.
Narayan
Kartik
K
Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, 751 23 Uppsala, Sweden.
Chumnarnsilpa
Sakesit
S
Choe
Han
H
Irobi
Edward
E
Urosev
Dunja
D
Lindberg
Uno
U
Schutt
Clarence E
CE
Burtnick
Leslie D
LD
Robinson
Robert C
RC
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D018360:Crystallography, X-Ray; D018260:Gelsolin / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011817:Rabbits
D000199:Actins; D018260:Gelsolin; D002118:Calcium