1rgi
From Proteopedia
(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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| - | [[Image:1rgi.gif|left|200px]]<br /><applet load="1rgi" size=" | + | [[Image:1rgi.gif|left|200px]]<br /><applet load="1rgi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rgi, resolution 3.00Å" /> | caption="1rgi, resolution 3.00Å" /> | ||
'''Crystal structure of gelsolin domains G1-G3 bound to actin'''<br /> | '''Crystal structure of gelsolin domains G1-G3 bound to actin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The actin filament-severing functionality of gelsolin resides in its | + | 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== | ==About this Structure== | ||
| - | 1RGI is a [http://en.wikipedia.org/wiki/Protein_complex 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] with CA and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RGI is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burtnick, L | + | [[Category: Burtnick, L D.]] |
[[Category: Irobi, E.]] | [[Category: Irobi, E.]] | ||
[[Category: Narayan, K.]] | [[Category: Narayan, K.]] | ||
| - | [[Category: Robinson, R | + | [[Category: Robinson, R C.]] |
[[Category: Urosev, D.]] | [[Category: Urosev, D.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: domain movement]] | [[Category: domain movement]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:39 2008'' |
Revision as of 12:50, 21 February 2008
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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 and 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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