1cof: Difference between revisions

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[[Image:1cof.jpg|left|200px]]


{{Structure
==YEAST COFILIN, ORTHORHOMBIC CRYSTAL FORM==
|PDB= 1cof |SIZE=350|CAPTION= <scene name='initialview01'>1cof</scene>, resolution 2.3&Aring;
<StructureSection load='1cof' size='340' side='right'caption='[[1cof]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND=
<table><tr><td colspan='2'>[[1cof]] 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=1COF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COF FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cof OCA], [https://pdbe.org/1cof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cof RCSB], [https://www.ebi.ac.uk/pdbsum/1cof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cof ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''YEAST COFILIN, ORTHORHOMBIC CRYSTAL FORM'''
[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 ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
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.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cof_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1COF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COF OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1cof ConSurf].
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:[http://www.ncbi.nlm.nih.gov/pubmed/9145106 9145106]
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Almo SC]]
[[Category: Almo, S C.]]
[[Category: Drubin DG]]
[[Category: Drubin, D G.]]
[[Category: Fedorov AA]]
[[Category: Fedorov, A A.]]
[[Category: Fedorov EV]]
[[Category: Fedorov, E V.]]
[[Category: Lappalainen P]]
[[Category: Lappalainen, P.]]
[[Category: actin-binding]]
[[Category: cytoskeleton]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:52 2008''

Latest revision as of 09:44, 7 February 2024

YEAST COFILIN, ORTHORHOMBIC CRYSTAL FORMYEAST COFILIN, ORTHORHOMBIC CRYSTAL FORM

Structural highlights

1cof is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ 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
  2. ↑ 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

1cof, resolution 2.30Å

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