PDBsum entry 1cfy

Actin-binding protein

PDB id

1cfy

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Contents

			Protein chains

					133 a.a. *

			Waters ×56

* Residue conservation analysis

PDB id:

1cfy

Links

Name:

Actin-binding protein

Title:

Yeast cofilin, monoclinic crystal form

Structure:

Cofilin. Chain: a, b. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.30Å

R-factor:

0.175

Authors:

A.A.Fedorov,P.Lappalainen,E.V.Fedorov,D.G.Drubin,S.C.Almo

Key ref:

A.A.Fedorov et al. (1997). Structure determination of yeast cofilin. Nat Struct Biol, 4, 366-369. PubMed id: 9145106

Date:

26-Nov-96

Release date:

01-Apr-97

PROCHECK

	Headers

	References

Protein chains

Q03048 (COFI_YEAST) - Cofilin from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:					143 a.a. 133 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Nat Struct Biol 4:366-369 (1997)
PubMed id: 9145106

Structure determination of yeast cofilin.
A.A.Fedorov, P.Lappalainen, E.V.Fedorov, D.G.Drubin, S.C.Almo.

ABSTRACT

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20368459

J.Pfaendtner, E.M.De La Cruz, and G.A.Voth (2010).
Actin filament remodeling by actin depolymerization factor/cofilin.

Proc Natl Acad Sci U S A, 107, 7299-7304.

20446344

S.H.Lee, and R.Dominguez (2010).
Regulation of actin cytoskeleton dynamics in cells.

Mol Cells, 29, 311-325.

20042603

S.Mehta, and L.D.Sibley (2010).
Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.

J Biol Chem, 285, 6835-6847.

18258262

E.E.Grintsevich, S.A.Benchaar, D.Warshaviak, P.Boontheung, F.Halgand, J.P.Whitelegge, K.F.Faull, R.R.Loo, D.Sept, J.A.Loo, and E.Reisler (2008).
Mapping the cofilin binding site on yeast G-actin by chemical cross-linking.

J Mol Biol, 377, 395-409.

18042684

J.K.Kamal, and M.R.Chance (2008).
Modeling of protein binary complexes using structural mass spectrometry data.

Protein Sci, 17, 79-94.

18625842

V.O.Paavilainen, E.Oksanen, A.Goldman, and P.Lappalainen (2008).
Structure of the actin-depolymerizing factor homology domain in complex with actin.

J Cell Biol, 182, 51-59.

PDB code:

3daw

17470807

J.K.Kamal, S.A.Benchaar, K.Takamoto, E.Reisler, and M.R.Chance (2007).
Three-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.

Proc Natl Acad Sci U S A, 104, 7910-7915.

17565945

N.Ren, J.Charlton, and P.N.Adler (2007).
The flare gene, which encodes the AIP1 protein of Drosophila, functions to regulate F-actin disassembly in pupal epidermal cells.

Genetics, 176, 2223-2234.

17360616

V.O.Paavilainen, M.Hellman, E.Helfer, M.Bovellan, A.Annila, M.F.Carlier, P.Permi, and P.Lappalainen (2007).
Structural basis and evolutionary origin of actin filament capping by twinfilin.

Proc Natl Acad Sci U S A, 104, 3113-3118.

PDB code:

2hd7

15735338

B.V.Strokopytov, A.Fedorov, N.M.Mahoney, M.Kessels, D.G.Drubin, and S.C.Almo (2005).
Phased translation function revisited: structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches.

Acta Crystallogr D Biol Crystallogr, 61, 285-293.

PDB code:

1hqz

15975905

H.Schüler, A.K.Mueller, and K.Matuschewski (2005).
A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers.

Mol Biol Cell, 16, 4013-4023.

15872087

O.Quintero-Monzon, A.A.Rodal, B.Strokopytov, S.C.Almo, and B.L.Goode (2005).
Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.

Mol Biol Cell, 16, 3128-3139.

14627701

B.J.Pope, K.M.Zierler-Gould, R.Kühne, A.G.Weeds, and L.J.Ball (2004).
Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor.

J Biol Chem, 279, 4840-4848.

PDB codes:

1q8g 1q8x

15501675

R.Dominguez (2004).
Actin-binding proteins--a unifying hypothesis.

Trends Biochem Sci, 29, 572-578.

15459340

X.Li, X.Liu, Z.Lou, X.Duan, H.Wu, Y.Liu, and Z.Rao (2004).
Crystal structure of human coactosin-like protein at 1.9 A resolution.

Protein Sci, 13, 2845-2851.

PDB code:

1vfq

12517699

S.J.Winder (2003).
Structural insights into actin-binding, branching and bundling proteins.

Curr Opin Cell Biol, 15, 14-22.

14621980

S.Ono (2003).
Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.

Biochemistry, 42, 13363-13370.

11980480

J.Q.Guan, S.Vorobiev, S.C.Almo, and M.R.Chance (2002).
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.

Biochemistry, 41, 5765-5775.

12049672

S.K.Maciver, and P.J.Hussey (2002).
The ADF/cofilin family: actin-remodeling proteins.

Genome Biol, 3, reviews3007.

12207032

V.O.Paavilainen, M.C.Merckel, S.Falck, P.J.Ojala, E.Pohl, M.Wilmanns, and P.Lappalainen (2002).
Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin.

J Biol Chem, 277, 43089-43095.

PDB code:

1m4j

11737197

L.Blondin, V.Sapountzi, S.K.Maciver, C.Renoult, Y.Benyamin, and C.Roustan (2001).
The second ADF/cofilin actin-binding site exists in F-actin, the cofilin-G-actin complex, but not in G-actin.

Eur J Biochem, 268, 6426-6434.

10662778

A.Y.Chan, M.Bailly, N.Zebda, J.E.Segall, and J.S.Condeelis (2000).
Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion.

J Cell Biol, 148, 531-542.

11025548

G.D.Bowman, I.M.Nodelman, Y.Hong, N.H.Chua, U.Lindberg, and C.E.Schutt (2000).
A comparative structural analysis of the ADF/cofilin family.

Proteins, 41, 374-384.

PDB code:

1f7s

11015196

M.Van Troys, D.Dewitte, J.L.Verschelde, M.Goethals, J.Vandekerckhove, and C.Ampe (2000).
The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant.

Biochemistry, 39, 12181-12189.

10366597

A.A.Rodal, J.W.Tetreault, P.Lappalainen, D.G.Drubin, and D.C.Amberg (1999).
Aip1p interacts with cofilin to disassemble actin filaments.

J Cell Biol, 145, 1251-1264.

10074138

B.Liu, R.Dai, C.J.Tian, L.Dawson, R.Gorelick, and X.F.Yu (1999).
Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin.

J Virol, 73, 2901-2908.

10506133

C.Renoult, D.Ternent, S.K.Maciver, A.Fattoum, C.Astier, Y.Benyamin, and C.Roustan (1999).
The identification of a second cofilin binding site on actin suggests a novel, intercalated arrangement of F-actin binding.

J Biol Chem, 274, 28893-28899.

10611961

J.R.Bamburg (1999).
Proteins of the ADF/cofilin family: essential regulators of actin dynamics.

Annu Rev Cell Dev Biol, 15, 185-230.

10581248

K.Moriyama, and I.Yahara (1999).
Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix.

EMBO J, 18, 6752-6761.

10567336

M.F.Carlier, F.Ressad, and D.Pantaloni (1999).
Control of actin dynamics in cell motility. Role of ADF/cofilin.

J Biol Chem, 274, 33827-33830.

9990286

M.Van Troys, J.Vandekerckhove, and C.Ampe (1999).
Structural modules in actin-binding proteins: towards a new classification.

Biochim Biophys Acta, 1448, 323-348.

10225951

S.Ono, D.L.Baillie, and G.M.Benian (1999).
UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle.

J Cell Biol, 145, 491-502.

9631289

A.McGough (1998).
F-actin-binding proteins.

Curr Opin Struct Biol, 8, 166-176.

9669865

A.P.Smertenko, C.J.Jiang, N.J.Simmons, A.G.Weeds, D.R.Davies, and P.J.Hussey (1998).
Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity.

Plant J, 14, 187-193.

9700161

B.L.Goode, D.G.Drubin, and P.Lappalainen (1998).
Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein.

J Cell Biol, 142, 723-733.

9694836

F.Ressad, D.Didry, G.X.Xia, Y.Hong, N.H.Chua, D.Pantaloni, and M.F.Carlier (1998).
Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation.

J Biol Chem, 273, 20894-20902.

9693358

P.Lappalainen, M.M.Kessels, M.J.Cope, and D.G.Drubin (1998).
The ADF homology (ADF-H) domain: a highly exploited actin-binding module.

Mol Biol Cell, 9, 1951-1959.

9452511

S.Ono, and G.M.Benian (1998).
Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics.

J Biol Chem, 273, 3778-3783.

9484592

Y.A.Puius, N.M.Mahoney, and S.C.Almo (1998).
The modular structure of actin-regulatory proteins.

Curr Opin Cell Biol, 10, 23-34.

9265645

A.McGough, B.Pope, W.Chiu, and A.Weeds (1997).
Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function.

J Cell Biol, 138, 771-781.

9275236

C.J.Jiang, A.G.Weeds, S.Khan, and P.J.Hussey (1997).
F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF).

Proc Natl Acad Sci U S A, 94, 9973-9978.

9407048

M.Van Troys, D.Dewitte, J.L.Verschelde, M.Goethals, J.Vandekerckhove, and C.Ampe (1997).
Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship.

J Biol Chem, 272, 32750-32758.

9312011

P.Lappalainen, E.V.Fedorov, A.A.Fedorov, S.C.Almo, and D.G.Drubin (1997).
Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis.

EMBO J, 16, 5520-5530.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.