|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1cfy' size='340' side='right'caption='[[1cfy]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1cfy' size='340' side='right'caption='[[1cfy]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1cfy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CFY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cfy]] 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=1CFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFY FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfy OCA], [http://pdbe.org/1cfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cfy RCSB], [http://www.ebi.ac.uk/pdbsum/1cfy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfy ProSAT]</span></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]] 2.3Å</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=1cfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfy OCA], [https://pdbe.org/1cfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfy RCSB], [https://www.ebi.ac.uk/pdbsum/1cfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 33: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Almo, S C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Drubin, D G]] | + | [[Category: Almo SC]] |
| - | [[Category: Fedorov, A A]] | + | [[Category: Drubin DG]] |
| - | [[Category: Fedorov, E V]] | + | [[Category: Fedorov AA]] |
| - | [[Category: Lappalainen, P]] | + | [[Category: Fedorov EV]] |
| - | [[Category: Actin-binding]] | + | [[Category: Lappalainen P]] |
| - | [[Category: Actin-binding protein]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| Structural highlights
Function
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.[1] [2]
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
Cofilin, a ubiquitous 15,000 M(r) protein, plays a central role in regulating cytoskeletal dynamics. Cofilin binds to actin monomers and filaments, and has a pH-dependent actin severing activity. The structure will allow for a detailed analysis of cofilin function.
Structure determination of yeast cofilin.,Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC Nat Struct Biol. 1997 May;4(5):366-9. PMID:9145106[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Iida K, Yahara I. Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells. 1999 Jan;4(1):21-32. PMID:10231390
- ↑ Ojala PJ, Paavilainen V, Lappalainen P. Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry. 2001 Dec 25;40(51):15562-9. PMID:11747431
- ↑ Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC. Structure determination of yeast cofilin. Nat Struct Biol. 1997 May;4(5):366-9. PMID:9145106
|
