1rgi
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1rgi |SIZE=350|CAPTION= <scene name='initialview01'>1rgi</scene>, resolution 3.00Å | |PDB= 1rgi |SIZE=350|CAPTION= <scene name='initialview01'>1rgi</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1p8z|1P8Z]], [[1p8x|1P8X]], [[1d0n|1D0N]], [[1h1v|1H1V]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgi OCA], [http://www.ebi.ac.uk/pdbsum/1rgi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rgi RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Robinson, R C.]] | [[Category: Robinson, R C.]] | ||
[[Category: Urosev, D.]] | [[Category: Urosev, D.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: CA]] | ||
[[Category: domain movement]] | [[Category: domain movement]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:27:52 2008'' |
Revision as of 20:27, 30 March 2008
| |||||||
| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1P8Z, 1P8X, 1D0N, 1H1V
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 23:27:52 2008
