1rgi
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(New page: 200px<br /><applet load="1rgi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgi, resolution 3.00Å" /> '''Crystal structure of...)
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Revision as of 23:27, 20 November 2007
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Crystal structure of gelsolin domains G1-G3 bound to actin
Overview
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.
About this Structure
1RGI is a Protein complex structure of sequences from Equus caballus and Oryctolagus cuniculus with CA and ATP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF., Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC, EMBO J. 2004 Jul 21;23(14):2713-22. Epub 2004 Jun 24. PMID:15215896
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