1qpv: Difference between revisions

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<StructureSection load='1qpv' size='340' side='right'caption='[[1qpv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1qpv' size='340' side='right'caption='[[1qpv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QPV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qpv]] 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=1QPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPV FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfy|1cfy]], [[1cof|1cof]]</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]] 3&#8491;</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=1qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpv OCA], [http://pdbe.org/1qpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qpv RCSB], [http://www.ebi.ac.uk/pdbsum/1qpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpv 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=1qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpv OCA], [https://pdbe.org/1qpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpv RCSB], [https://www.ebi.ac.uk/pdbsum/1qpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpv 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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[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 protein]]
[[Category: Lappalainen P]]
[[Category: Cofilin fold]]
[[Category: Three layers:alpha/mixed beta/alpha]]

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