4kef
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4kef is ON HOLD Authors: Kish-Trier, E., Haarer, B., Cingolani, G., Amberg, D.C. Description: Structure of Cofilin Mutant (cof1-159p)) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Cofilin Mutant (cof1-159p)== | |
| - | + | <StructureSection load='4kef' size='340' side='right'caption='[[4kef]], [[Resolution|resolution]] 1.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4kef]] is a 1 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=4KEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KEF 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]] 1.098Å</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=4kef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kef OCA], [https://pdbe.org/4kef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kef RCSB], [https://www.ebi.ac.uk/pdbsum/4kef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kef ProSAT]</span></td></tr> | ||
| + | </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__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Amberg DC]] | ||
| + | [[Category: Cingolani G]] | ||
| + | [[Category: Haarer B]] | ||
| + | [[Category: Kish-Trier E]] | ||
Current revision
Structure of Cofilin Mutant (cof1-159p)
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