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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 3.00&Aring;" /> '''Crystal structure of...)
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[[Image:1rgi.gif|left|200px]]<br /><applet load="1rgi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rgi, resolution 3.00&Aring;" />
 
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'''Crystal structure of gelsolin domains G1-G3 bound to actin'''<br />
 
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==Overview==
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==Crystal structure of gelsolin domains G1-G3 bound to actin==
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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.
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<StructureSection load='1rgi' size='340' side='right'caption='[[1rgi]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rgi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RGI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgi OCA], [https://pdbe.org/1rgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgi RCSB], [https://www.ebi.ac.uk/pdbsum/1rgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GELS_HORSE GELS_HORSE] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rgi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rgi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15215896</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RGI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15215896 15215896]
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</div>
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<div class="pdbe-citations 1rgi" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Actin 3D structures|Actin 3D structures]]
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*[[Gelsolin 3D structures|Gelsolin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
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[[Category: Burtnick LD]]
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[[Category: Burtnick, L.D.]]
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[[Category: Irobi E]]
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[[Category: Irobi, E.]]
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[[Category: Narayan K]]
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[[Category: Narayan, K.]]
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[[Category: Robinson RC]]
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[[Category: Robinson, R.C.]]
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[[Category: Urosev D]]
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[[Category: Urosev, D.]]
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[[Category: ATP]]
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[[Category: CA]]
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[[Category: domain movement]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:34:45 2007''
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Current revision

Crystal structure of gelsolin domains G1-G3 bound to actin

PDB ID 1rgi

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