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Actin binding protein PDB id
1ahq
Jmol
Contents
Protein chain
133 a.a. *
Waters ×213
* Residue conservation analysis
PDB id:
1ahq
Name: Actin binding protein
Title: Recombinant actophorin
Structure: Actophorin. Chain: a. Engineered: yes
Source: Acanthamoeba castellanii. Organism_taxid: 5755. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.30Å     R-factor:   0.210     R-free:   0.320
Authors: S.A.Leonard,A.G.Gittis,E.C.Petrella,T.D.Pollard,E.E.Lattman
Key ref: S.A.Leonard et al. (1997). Crystal structure of the actin-binding protein actophorin from Acanthamoeba. Nat Struct Biol, 4, 369-373. PubMed id: 9145107 DOI: 10.1038/nsb0597-369
Date:
10-Apr-97     Release date:   04-Sep-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P37167  (ACTP_ACACA) -  Actophorin
Seq:
Struc:
138 a.a.
133 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   2 terms 
  Biochemical function     actin binding     1 term  

 

 
DOI no: 10.1038/nsb0597-369 Nat Struct Biol 4:369-373 (1997)
PubMed id: 9145107  
 
 
Crystal structure of the actin-binding protein actophorin from Acanthamoeba.
S.A.Leonard, A.G.Gittis, E.C.Petrella, T.D.Pollard, E.E.Lattman.
 
  ABSTRACT  
 
Actophorin is a member of the actin-depolymerizing factor/cofilin family. It severs actin filaments and sequesters actin monomers. The crystal structure of actophorin will help to elucidate actin-ADF/cofilin interactions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
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
14992720 E.J.McGhie, R.D.Hayward, and V.Koronakis (2004).
Control of actin turnover by a salmonella invasion protein.
  Mol Cell, 13, 497-510.  
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.  
  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.  
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.  
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.  
10551802 H.N.Higgs, and T.D.Pollard (1999).
Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins.
  J Biol Chem, 274, 32531-32534.  
10611961 J.R.Bamburg (1999).
Proteins of the ADF/cofilin family: essential regulators of actin dynamics.
  Annu Rev Cell Dev Biol, 15, 185-230.  
10461190 J.R.Bamburg, A.McGough, and S.Ono (1999).
Putting a new twist on actin: ADF/cofilins modulate actin dynamics.
  Trends Cell Biol, 9, 364-370.  
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.  
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.  
9737968 L.Blanchoin, and T.D.Pollard (1998).
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin.
  J Biol Chem, 273, 25106-25111.
PDB code: 1cnu
  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.  
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 codes are shown on the right.