1RGI

Crystal structure of gelsolin domains G1-G3 bound to actin

Summary for 1RGI

• Entry DOI: 10.2210/pdb1rgi/pdb
• Related: 1D0N 1H1V 1P8X 1P8Z
• Descriptor: Gelsolin, Actin, alpha skeletal muscle, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: domain movement, contractile protein
• Biological source: Equus caballus (horse); More
• Total number of polymer chains: 2
• Total formula weight: 81603.41

Authors

Burtnick, L.D.,Urosev, D.,Irobi, E.,Narayan, K.,Robinson, R.C. (deposition date: 2003-11-12, release date: 2004-07-27, Last modification date: 2023-08-23)

Primary citation

Burtnick, L.D.,Urosev, D.,Irobi, E.,Narayan, K.,Robinson, R.C.
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF
Embo J., 23:2713-2722, 2004

PubMed Abstract: The actin filament-severing functionality of gelsolin resides in its N-terminal three domains (G1-G3). We have determined the structure of this fragment in complex with an actin monomer. The structure reveals the dramatic domain rearrangements that activate G1-G3, which include the replacement of interdomain interactions observed in the inactive, calcium-free protein by new contacts to actin, and by a novel G2-G3 interface. Together, these conformational changes are critical for actin filament severing, and we suggest that their absence leads to the disease Finnish-type familial amyloidosis. Furthermore, we propose that association with actin drives the calcium-independent activation of isolated G1-G3 during apoptosis, and that a similar mechanism operates to activate native gelsolin at micromolar levels of calcium. This is the first structure of a filament-binding protein bound to actin and it sets stringent, high-resolution limitations on the arrangement of actin protomers within the filament.

PubMed: 15215896
DOI: 10.1038/sj.emboj.7600280

Experimental method

X-RAY DIFFRACTION (3 Å)