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PDBsum entry 1ksr
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Actin binding protein PDB id
1ksr

 

 

 

 

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Contents
Protein chain
100 a.a. *
* Residue conservation analysis
PDB id:
1ksr
Name: Actin binding protein
Title: The repeating segments of the f-actin cross-linking gelation factor (abp-120) have an immunoglobulin fold, nmr, 20 structures
Structure: Gelation factor. Chain: a. Fragment: rod 4. Synonym: abp-120. Engineered: yes
Source: Dictyostelium discoideum. Organism_taxid: 44689. Strain: ax3. Cell_line: bl21. Cellular_location: cytoplasm, cell cortex. Gene: abpc. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: P.Fucini,C.Renner,C.Herberhold,A.A.Noegel,T.A.Holak
Key ref: P.Fucini et al. (1997). The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold. Nat Struct Biol, 4, 223-230. PubMed id: 9164464
Date:
07-Feb-97     Release date:   20-Aug-97    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13466  (GELA_DICDI) -  Gelation factor from Dictyostelium discoideum
Seq:
Struc: 		 
Seq:
Struc: 		857 a.a.
100 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 4:223-230 (1997)
PubMed id: 9164464  
 
 
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.
P.Fucini, C.Renner, C.Herberhold, A.A.Noegel, T.A.Holak.
 
  ABSTRACT  
 
The 120,000 M(r) gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are rod-shaped homodimers. Each monomer chain is comprised of an actin-binding domain and a rod domain. The rod domain of the gelation factor consists of six 100-residue repetitive segments with high internal homology. We have now determined the three-dimensional structure of segment 4 of the rod domain of the gelation factor from D. discoideum using NMR spectroscopy. The segment consists of seven beta-sheets arranged in an immunoglobulin-like (Ig) fold. This is completely different from the alpha-actinin rod domain which consists of four spectrin-like alpha-helical segments. The gelation factor is the first example of an Ig-fold found in an actin-binding protein. Two highly homologous actin-binding proteins from human with similar sequences to the gelation factor, filamin and a 280,000 M(r) actin-binding protein (ABP-280), share conserved residues that form the core of the gelation factor repetitive segment structure. Thus, the segment 4 structure should be common to this subfamily of the spectrin superfamily. The structure of segment 4 together with previously published electron microscopy data, provide an explanation for the dimerization of the whole gelation factor molecule.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21496645 M.E.Aubin-Tam, A.O.Olivares, R.T.Sauer, T.A.Baker, and M.J.Lang (2011).
Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.
  Cell, 145, 257-267.  
19805437 B.A.Kesner, S.L.Milgram, B.R.Temple, and N.V.Dokholyan (2010).
Isoform divergence of the filamin family of proteins.
  Mol Biol Evol, 27, 283-295.  
19466753 C.A.Otey, R.Dixon, C.Stack, and S.M.Goicoechea (2009).
Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human disease.
  Cell Motil Cytoskeleton, 66, 618-634.  
18266910 H.Xiong, F.Rivero, U.Euteneuer, S.Mondal, S.Mana-Capelli, D.Larochelle, A.Vogel, B.Gassen, and A.A.Noegel (2008).
Dictyostelium Sun-1 connects the centrosome to chromatin and ensures genome stability.
  Traffic, 9, 708-724.  
18180288 R.D.Dixon, D.K.Arneman, A.S.Rachlin, N.R.Sundaresan, M.J.Costello, S.L.Campbell, and C.A.Otey (2008).
Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin.
  J Biol Chem, 283, 6222-6231.  
17987659 W.B.Holmes, and C.L.Moncman (2008).
Nebulette interacts with filamin C.
  Cell Motil Cytoskeleton, 65, 130-142.  
  17401197 A.H.Aguda, A.M.Sakwe, L.Rask, and R.C.Robinson (2007).
Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 291-293.  
18056414 F.Nakamura, T.M.Osborn, C.A.Hartemink, J.H.Hartwig, and T.P.Stossel (2007).
Structural basis of filamin A functions.
  J Cell Biol, 179, 1011-1025.  
17121815 N.Khaire, R.Müller, R.Blau-Wasser, L.Eichinger, M.Schleicher, M.Rief, T.A.Holak, and A.A.Noegel (2007).
Filamin-regulated F-actin assembly is essential for morphogenesis and controls phototaxis in Dictyostelium.
  J Biol Chem, 282, 1948-1955.  
17690686 Y.Lad, T.Kiema, P.Jiang, O.T.Pentikäinen, C.H.Coles, I.D.Campbell, D.A.Calderwood, and J.Ylänne (2007).
Structure of three tandem filamin domains reveals auto-inhibition of ligand binding.
  EMBO J, 26, 3993-4004.
PDB code: 2j3s
16781869 G.M.Popowicz, M.Schleicher, A.A.Noegel, and T.A.Holak (2006).
Filamins: promiscuous organizers of the cytoskeleton.
  Trends Biochem Sci, 31, 411-419.  
15731336 E.Y.Levanon, M.Hallegger, Y.Kinar, R.Shemesh, K.Djinovic-Carugo, G.Rechavi, M.F.Jantsch, and E.Eisenberg (2005).
Evolutionarily conserved human targets of adenosine to inosine RNA editing.
  Nucleic Acids Res, 33, 1162-1168.  
15608615 I.Schwaiger, M.Schleicher, A.A.Noegel, and M.Rief (2005).
The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.
  EMBO Rep, 6, 46-51.  
15642266 R.Pudas, T.R.Kiema, P.J.Butler, M.Stewart, and J.Ylänne (2005).
Structural basis for vertebrate filamin dimerization.
  Structure, 13, 111-119.
PDB code: 1v05
15531635 H.Dietz, and M.Rief (2004).
Exploring the energy landscape of GFP by single-molecule mechanical experiments.
  Proc Natl Acad Sci U S A, 101, 16192-16197.  
14718927 I.Schwaiger, A.Kardinal, M.Schleicher, A.A.Noegel, and M.Rief (2004).
A mechanical unfolding intermediate in an actin-crosslinking protein.
  Nat Struct Mol Biol, 11, 81-85.  
15159586 L.Sjekloća, B.Sjöblom, M.Polentarutti, and K.Djinović Carugo (2004).
Cloning, expression, purification, crystallization and preliminary crystallographic analysis of gamma-filamin repeat 23.
  Acta Crystallogr D Biol Crystallogr, 60, 1155-1157.  
14988809 M.Zenker, A.Rauch, A.Winterpacht, A.Tagariello, C.Kraus, T.Rupprecht, H.Sticht, and A.Reis (2004).
A dual phenotype of periventricular nodular heterotopia and frontometaphyseal dysplasia in one patient caused by a single FLNA mutation leading to two functionally different aberrant transcripts.
  Am J Hum Genet, 74, 731-737.  
15068803 R.J.Gilbert, P.Fucini, S.Connell, S.D.Fuller, K.H.Nierhaus, C.V.Robinson, C.M.Dobson, and D.I.Stuart (2004).
Three-dimensional structures of translating ribosomes by Cryo-EM.
  Mol Cell, 14, 57-66.  
12871294 J.Hartwig, and J.Italiano (2003).
The birth of the platelet.
  J Thromb Haemost, 1, 1580-1586.  
12112706 A.K.Felts, E.Gallicchio, A.Wallqvist, and R.M.Levy (2002).
Distinguishing native conformations of proteins from decoys with an effective free energy estimator based on the OPLS all-atom force field and the Surface Generalized Born solvent model.
  Proteins, 48, 404-422.  
11807098 A.van der Flier, I.Kuikman, D.Kramer, D.Geerts, M.Kreft, T.Takafuta, S.S.Shapiro, and A.Sonnenberg (2002).
Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits.
  J Cell Biol, 156, 361-376.  
11336782 A.van der Flier, and A.Sonnenberg (2001).
Structural and functional aspects of filamins.
  Biochim Biophys Acta, 1538, 99.  
11153914 C.Chakarova, M.S.Wehnert, K.Uhl, S.Sakthivel, H.P.Vosberg, P.F.van der Ven, and D.O.Fürst (2000).
Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family.
  Hum Genet, 107, 597-611.  
10391919 A.E.El-Husseini, and S.R.Vincent (1999).
Cloning and characterization of a novel RING finger protein that interacts with class V myosins.
  J Biol Chem, 274, 19771-19777.  
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.  
9700162 F.Rivero, A.Kuspa, R.Brokamp, M.Matzner, and A.A.Noegel (1998).
Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments.
  J Cell Biol, 142, 735-750.  
9817844 S.Bañuelos, M.Saraste, and K.Djinović Carugo (1998).
Structural comparisons of calponin homology domains: implications for actin binding.
  Structure, 6, 1419-1431.
PDB code: 1bkr
9651345 T.Takafuta, G.Wu, G.F.Murphy, and S.S.Shapiro (1998).
Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha.
  J Biol Chem, 273, 17531-17538.  
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.  
9480045 P.R.Fisher, A.A.Noegel, M.Fechheimer, F.Rivero, J.Prassler, and G.Gerisch (1997).
Photosensory and thermosensory responses in Dictyostelium slugs are specifically impaired by absence of the F-actin cross-linking gelation factor (ABP-120).
  Curr Biol, 7, 889-892.  
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.

 

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