1rgi: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 4: Line 4:
|PDB= 1rgi |SIZE=350|CAPTION= <scene name='initialview01'>1rgi</scene>, resolution 3.00&Aring;
|PDB= 1rgi |SIZE=350|CAPTION= <scene name='initialview01'>1rgi</scene>, resolution 3.00&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
Line 32: Line 32:
[[Category: domain movement]]
[[Category: domain movement]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:19 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:28:33 2008''

Revision as of 14:28, 23 March 2008

File:1rgi.gif


PDB ID 1rgi

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of gelsolin domains G1-G3 bound to actin


OverviewOverview

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 StructureAbout this Structure

1RGI is a Protein complex structure of sequences from Equus caballus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

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 23 13:28:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA