2acg
From Proteopedia
(Difference between revisions)
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<StructureSection load='2acg' size='340' side='right'caption='[[2acg]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2acg' size='340' side='right'caption='[[2acg]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2acg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2acg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ACG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2acg OCA], [https://pdbe.org/2acg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2acg RCSB], [https://www.ebi.ac.uk/pdbsum/2acg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2acg 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=2acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2acg OCA], [https://pdbe.org/2acg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2acg RCSB], [https://www.ebi.ac.uk/pdbsum/2acg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2acg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PROF2_ACACA PROF2_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2acg ConSurf]. | </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=2acg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin. | ||
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| - | X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.,Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:8078936<ref>PMID:8078936</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2acg" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Profilin 3D Structures|Profilin 3D Structures]] | *[[Profilin 3D Structures|Profilin 3D Structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acanthamoeba castellanii]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Fedorov | + | [[Category: Fedorov AA]] |
| - | [[Category: Graupe | + | [[Category: Graupe MH]] |
| - | [[Category: Lattman | + | [[Category: Lattman EE]] |
| - | [[Category: Magnus | + | [[Category: Magnus KA]] |
| - | [[Category: Pollard | + | [[Category: Pollard TD]] |
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Current revision
ACANTHAMOEBA CASTELLANII PROFILIN II
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