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1pgu

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(New page: 200px<br /><applet load="1pgu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pgu, resolution 2.30&Aring;" /> '''YEAST ACTIN INTERACT...)
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[[Image:1pgu.gif|left|200px]]<br /><applet load="1pgu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pgu, resolution 2.30&Aring;" />
 
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'''YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM'''<br />
 
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==Overview==
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==YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM==
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Actin-interacting protein 1 (Aip1p) is a 67-kDa WD repeat protein known to, regulate the depolymerization of actin filaments by cofilin and is, conserved in organisms ranging from yeast to mammals. The crystal, structure of Aip1p from Saccharomyces cerevisiae was determined to a 2.3-A, resolution and a final crystallographic R-factor of 0.204. The structure, reveals that the overall fold is formed by two connected seven-bladed, beta-propellers and has important implications for the structure of Aip1, from other organisms and WD repeat-containing proteins in general. These, results were unexpected because a maximum of 10 WD repeats had been, reported in the literature for this protein using sequence data. The, surfaces of the beta-propellers formed by the D-A and B-C loops are, positioned adjacent to one another, giving Aip1p a shape that resembles an, open "clamshell." The mapping of conserved residues to the structure of, Aip1p reveals dense patches of conserved residues on the surface of one, beta-propeller and at the interface of the two beta-propellers. These two, patches of conserved residues suggest a potential binding site for F-actin, on Aip1p and that the orientation of the beta-propellers with respect to, one another plays a role in binding an actin-cofilin complex. In addition, the conserved interface between the domains is mediated by a number of, interactions that appear to impart rigidity between the two domains of, Aip1p and may make a large substrate-induced conformational change, difficult.
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<StructureSection load='1pgu' size='340' side='right'caption='[[1pgu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1pgu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PGU FirstGlance]. <br>
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1PGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PGU OCA].
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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]] 2.3&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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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=1pgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pgu OCA], [https://pdbe.org/1pgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pgu RCSB], [https://www.ebi.ac.uk/pdbsum/1pgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pgu ProSAT]</span></td></tr>
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The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization., Voegtli WC, Madrona AY, Wilson DK, J Biol Chem. 2003 Sep 5;278(36):34373-9. Epub 2003 Jun 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12807914 12807914]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AIP1_YEAST AIP1_YEAST] Involved in the depolymerization of actin filaments. Enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.<ref>PMID:10366597</ref>
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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/pg/1pgu_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=1pgu ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Madrona AY]]
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[[Category: Madrona, A.Y.]]
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[[Category: Voegtli WC]]
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[[Category: Voegtli, W.C.]]
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[[Category: Wilson DK]]
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[[Category: Wilson, D.K.]]
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[[Category: ZN]]
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[[Category: seven-bladed beta-propeller]]
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[[Category: wd repeat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:47:40 2007''
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Current revision

YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM

PDB ID 1pgu

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