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2i2q

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Revision as of 08:21, 18 October 2017

Fission Yeast cofilin

Structural highlights

2i2q is a 1 chain structure with sequence from Cbs 356. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1cof
Gene:	cof1 (CBS 356)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COFI_SCHPO] 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.^[1]

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

ADF/cofilins are key regulators of actin dynamics during cellular motility, yet their precise role and mechanism of action are shrouded in ambiguity. Direct observation of actin filaments by evanescent wave microscopy showed that cofilins from fission yeast and human do not increase the rate that pointed ends of actin filaments shorten beyond the rate for ADP-actin subunits, but both cofilins inhibit elongation and subunit dissociation at barbed ends. Direct observation also showed that cofilins from fission yeast, Acanthamoeba, and human sever actin filaments optimally at low-cofilin binding densities well below their K(d)s, but not at high binding densities. High concentrations of cofilin nucleate actin assembly. Thus, the action of cofilins in cells will depend on the local concentration of active cofilins: low concentrations favor severing, whereas high concentrations favor nucleation. These results establish a clear paradigm for actin turnover by cofilin in cells.

Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin.,Andrianantoandro E, Pollard TD Mol Cell. 2006 Oct 6;24(1):13-23. PMID:17018289^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakano K, Mabuchi I. Actin-depolymerizing protein Adf1 is required for formation and maintenance of the contractile ring during cytokinesis in fission yeast. Mol Biol Cell. 2006 Apr;17(4):1933-45. Epub 2006 Feb 8. PMID:16467379 doi:http://dx.doi.org/10.1091/mbc.E05-09-0900
↑ Andrianantoandro E, Pollard TD. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell. 2006 Oct 6;24(1):13-23. PMID:17018289 doi:10.1016/j.molcel.2006.08.006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i2q"

Categories: Cbs 356 | Andrianantoandro, E | Pollard, T D | Actin-binding protein | N-terminal serine

@@ Line 1: / Line 1: @@
 ==Fission Yeast cofilin==
 <StructureSection load='2i2q' size='340' side='right' caption='[[2i2q]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cof|1cof]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cof1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=2i2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2q OCA], [http://pdbe.org/2i2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i2q RCSB], [http://www.ebi.ac.uk/pdbsum/2i2q PDBsum]</span></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=2i2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2q OCA], [http://pdbe.org/2i2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i2q RCSB], [http://www.ebi.ac.uk/pdbsum/2i2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i2q ProSAT]</span></td></tr>
 </table>
 == Function ==

2i2q

From Proteopedia

Revision as of 08:21, 18 October 2017

Fission Yeast cofilin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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