1P8X

The Calcium-Activated C-terminal half of gelsolin

Summary for 1P8X

• Entry DOI: 10.2210/pdb1p8x/pdb
• Descriptor: Gelsolin precursor, plasma, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium-binding, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted: P06396
• Total number of polymer chains: 3
• Total formula weight: 113647.00

Authors

Narayan, K.,Burtnick, L.D.,Robinson, R.C. (deposition date: 2003-05-08, release date: 2003-10-14, Last modification date: 2023-08-16)

Primary citation

Narayan, K.,Chumnarnsilpa, S.,Choe, H.,Irobi, E.,Urosev, D.,Lindberg, U.,Schutt, C.E.,Burtnick, L.D.,Robinson, R.C.
Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin
FEBS LETT., 552:82-85, 2003

PubMed 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.

PubMed: 14527664
DOI: 10.1016/S0014-5793(03)00933-5

Experimental method

X-RAY DIFFRACTION (2 Å)