4ked
From Proteopedia
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==Crystal Structure of Cofilin Mutant (cof1-157p)== | ==Crystal Structure of Cofilin Mutant (cof1-157p)== | ||
| - | <StructureSection load='4ked' size='340' side='right' caption='[[4ked]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4ked' size='340' side='right'caption='[[4ked]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ked]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4ked]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KED 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]] 1.901Å</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=4ked FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ked OCA], [https://pdbe.org/4ked PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ked RCSB], [https://www.ebi.ac.uk/pdbsum/4ked PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ked ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COFI_YEAST COFI_YEAST] Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.<ref>PMID:10231390</ref> <ref>PMID:11747431</ref> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Saccharomyces cerevisiae | + | [[Category: Large Structures]] |
| - | [[Category: Amberg | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Cingolani | + | [[Category: Amberg DC]] |
| - | [[Category: Haarer | + | [[Category: Cingolani G]] |
| - | [[Category: Kish-Trier | + | [[Category: Haarer B]] |
| - | + | [[Category: Kish-Trier E]] | |
| - | + | ||
Current revision
Crystal Structure of Cofilin Mutant (cof1-157p)
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