1cfy

From Proteopedia

(Difference between revisions)

Revision as of 11:22, 24 August 2017

YEAST COFILIN, MONOCLINIC CRYSTAL FORM

Structural highlights

1cfy is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

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

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/1cfy"

@@ Line 1: / Line 1: @@
 ==YEAST COFILIN, MONOCLINIC CRYSTAL FORM==
 <StructureSection load='1cfy' size='340' side='right' caption='[[1cfy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cfy]] is a 2 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=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. 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>
-</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]</span></td></tr>
+</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>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1cfy ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Almo, S C]]
 [[Category: Drubin, D G]]

1cfy

From Proteopedia

Revision as of 11:22, 24 August 2017

YEAST COFILIN, MONOCLINIC CRYSTAL FORM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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