1pev: Difference between revisions
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==Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans== | |||
<StructureSection load='1pev' size='340' side='right'caption='[[1pev]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1pev]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pev OCA], [https://pdbe.org/1pev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pev RCSB], [https://www.ebi.ac.uk/pdbsum/1pev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pev ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1pev TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/WDR1_CAEEL WDR1_CAEEL] Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Regulator of actin organization in myofibrils. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1pev_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1pev ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping. | |||
Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.,Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269<ref>PMID:15150269</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1pev" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Almo SC]] | ||
[[Category: | [[Category: Burley SK]] | ||
[[Category: | [[Category: Fedorov AA]] | ||
[[Category: | [[Category: Mohri K]] | ||
[[Category: Ono | [[Category: Ono S]] | ||
[[Category: Vorobiev | [[Category: Vorobiev S]] | ||
Latest revision as of 12:42, 16 August 2023
Crystal Structure of the Actin Interacting Protein from Caenorhabditis ElegansCrystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans
Structural highlights
FunctionWDR1_CAEEL Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Regulator of actin organization in myofibrils. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedActin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping. Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.,Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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