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| | <StructureSection load='1pi6' size='340' side='right'caption='[[1pi6]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1pi6' size='340' side='right'caption='[[1pi6]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pi6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PI6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pi6]] is a 1 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=1PI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PI6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pgu|1pgu]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIP1 OR YMR092C OR YM9582.17C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1pi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi6 OCA], [https://pdbe.org/1pi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi6 ProSAT]</span></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=1pi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi6 OCA], [https://pdbe.org/1pi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pi6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pi6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Madrona, A Y]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Voegtli, W C]] | + | [[Category: Madrona AY]] |
| - | [[Category: Wilson, D K]] | + | [[Category: Voegtli WC]] |
| - | [[Category: Beta-propeller]] | + | [[Category: Wilson DK]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Wd repeat]]
| + | |
| Structural highlights
Function
AIP1_YEAST Involved in the depolymerization of actin filaments. Enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.[1]
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 PubMed
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.
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:12807914[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rodal AA, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC. Aip1p interacts with cofilin to disassemble actin filaments. J Cell Biol. 1999 Jun 14;145(6):1251-64. PMID:10366597
- ↑ Voegtli WC, Madrona AY, Wilson DK. The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization. J Biol Chem. 2003 Sep 5;278(36):34373-9. Epub 2003 Jun 14. PMID:12807914 doi:10.1074/jbc.M302773200
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