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1rgi
From Proteopedia
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| - | [[Image:1rgi.gif|left|200px]] | + | [[Image:1rgi.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of gelsolin domains G1-G3 bound to actin''' | + | {{Structure |
| + | |PDB= 1rgi |SIZE=350|CAPTION= <scene name='initialview01'>1rgi</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of gelsolin domains G1-G3 bound to actin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RGI is a [ | + | 1RGI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15215896 15215896] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: domain movement]] | [[Category: domain movement]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:19 2008'' |
Revision as of 11:51, 20 March 2008
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| , resolution 3.00Å | |||||||
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| Ligands: | and | ||||||
| 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 Thu Mar 20 13:51:19 2008
