PDBsum entry 1c0g

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Contractile protein PDB id
Protein chains
127 a.a. *
368 a.a. *
_CA ×3
Waters ×469
* Residue conservation analysis
PDB id:
Name: Contractile protein
Title: Crystal structure of 1:1 complex between gelsolin segment 1 and a dictyostelium/tetrahymena chimera actin (mutant 228: q228k/t229a/a230y/e360h)
Structure: Protein (gelsolin segment 1). Chain: s. Engineered: yes. Mutation: yes. Protein (chimeric actin). Chain: a. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: bacteria. Expression_system_taxid: 2. Dictyostelium discoideum, tetrahymena thermophila. ,. Organism_taxid: 44689,5911.
Biol. unit: Dimer (from PQS)
2.00Å     R-factor:   0.182     R-free:   0.223
Authors: Y.Matsuura,M.Stewart,M.Kawamoto,N.Kamiya,K.Saeki,T.Yasunaga, T.Wakabayashi
Key ref:
Y.Matsuura et al. (2000). Structural basis for the higher Ca(2+)-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras. J Mol Biol, 296, 579-595. PubMed id: 10669610 DOI: 10.1006/jmbi.1999.3467
16-Jul-99     Release date:   01-Mar-00    
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Protein chain
Pfam   ArchSchema ?
P06396  (GELS_HUMAN) -  Gelsolin
782 a.a.
127 a.a.*
Protein chain
Pfam   ArchSchema ?
P07830  (ACT1_DICDI) -  Major actin
376 a.a.
368 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell-cell contact zone   12 terms 
  Biological process     macropinocytosis   10 terms 
  Biochemical function     nucleotide binding     6 terms  


DOI no: 10.1006/jmbi.1999.3467 J Mol Biol 296:579-595 (2000)
PubMed id: 10669610  
Structural basis for the higher Ca(2+)-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras.
Y.Matsuura, M.Stewart, M.Kawamoto, N.Kamiya, K.Saeki, T.Yasunaga, T.Wakabayashi.
Replacement of residues 228-230 or 228-232 of subdomain 4 in Dictyostelium actin with the corresponding Tetrahymena sequence (QTA to KAY replacement: half chimera-1; QTAAS to KAYKE replacement: full chimera) leads to a higher Ca(2+)-activation of the regulated acto-myosin subfragment-1 ATPase activity. The ratio of ATPase activation in the presence of tropomyosin-troponin and Ca(2+) to that without tropomyosin-troponin becomes about four times as large as the ratio for the wild-type actin. To understand the structural basis of this higher Ca(2+)-activation, we have determined the crystal structures of the 1:1 complex of Dictyostelium mutant actins (half chimera-1 and full chimera) with gelsolin segment-1 to 2.0 A and 2.4 A resolution, respectively, together with the structure of wild-type actin as a control. Although there were local changes on the surface of the subdomain 4 and the phenolic side-chain of Tyr230 displaced the side-chain of Leu236 from a non-polar pocket to a more solvent-accessible position, the structures of the actin chimeras showed that the mutations in the 228-232 region did not introduce large changes in the overall actin structure. This suggests that residues near position 230 formed part of the tropomyosin binding site on actin in actively contracting muscle. The higher Ca(2+)-activation observed with A230Y-containing mutants can be understood in terms of a three-state model for thin filament regulation in which, in the presence of both Ca(2+) and myosin heads, the local changes of actin generated by the mutation (especially its phenolic side-chain) facilitate the transition of thin filaments from a "closed" state to an "open" state. Between 394 and 469 water molecules were identified in the different structures and it was found that actin recognizes hydrated forms of the adenine base and the Ca ion in the nucleotide binding site.
  Selected figure(s)  
Figure 2.
Figure 2. Overview of the crystal structure of the complex formed between wild-type Dictyostelium actin (yellow) and gelsolin segment 1 (light green). The ATP is shown as a ball-and-stick model and the calcium ions as orange spheres. Figure 2 and Figure 8 were prepared with the molecular graphics program MOLSCRIPT [Kraulis 1991].
Figure 7.
Figure 7. Schematic representation showing the interaction between Ca^2+ ATP and a mutant actin (half chimera-1). Water molecules (pink spheres) are important for mediating both the interaction between the adenine ring and actin and also for the binding of the Ca^2+ and phosphate. The adenine base fits in a hydrophobic pocket (yellow thick line) but many of its hydrogen-bonded interactions with polar groups on actin are mediated through water molecules. Similarly, the interactions of Ca^2+ to acidic residues on actin such as aspartate residues 11 and 154 are mediated through water molecules. Broken cyan lines correspond to hydrogen bonds or electrostatic interactions. The corresponding distances in Å are given next to the broken lines. The distance in Å between Wat203 and the g-phosphorous is also given next to a black arrow.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 296, 579-595) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20946985 K.Murakami, T.Yasunaga, T.Q.Noguchi, Y.Gomibuchi, K.X.Ngo, T.Q.Uyeda, and T.Wakabayashi (2010).
Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release.
  Cell, 143, 275-287.
PDB codes: 3a5l 3a5m 3a5n 3a5o 3g37
20033048 D.Wu, P.Hugenholtz, K.Mavromatis, R.Pukall, E.Dalin, N.N.Ivanova, V.Kunin, L.Goodwin, M.Wu, B.J.Tindall, S.D.Hooper, A.Pati, A.Lykidis, S.Spring, I.J.Anderson, P.D'haeseleer, A.Zemla, M.Singer, A.Lapidus, M.Nolan, A.Copeland, C.Han, F.Chen, J.F.Cheng, S.Lucas, C.Kerfeld, E.Lang, S.Gronow, P.Chain, D.Bruce, E.M.Rubin, N.C.Kyrpides, H.P.Klenk, and J.A.Eisen (2009).
A phylogeny-driven genomic encyclopaedia of Bacteria and Archaea.
  Nature, 462, 1056-1060.  
18515362 M.Iwasa, K.Maeda, A.Narita, Y.Maéda, and T.Oda (2008).
Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants.
  J Biol Chem, 283, 21045-21053.  
12732734 S.Vorobiev, B.Strokopytov, D.G.Drubin, C.Frieden, S.Ono, J.Condeelis, P.A.Rubenstein, and S.C.Almo (2003).
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.
  Proc Natl Acad Sci U S A, 100, 5760-5765.
PDB codes: 1d4x 1nlv 1nm1 1nmd 1yag
11459946 M.Stewart (2001).
Structural basis for bending tropomyosin around actin in muscle thin filaments.
  Proc Natl Acad Sci U S A, 98, 8165-8166.  
10747081 T.M.Roberts, and M.Stewart (2000).
Acting like actin. The dynamics of the nematode major sperm protein (msp) cytoskeleton indicate a push-pull mechanism for amoeboid cell motility.
  J Cell Biol, 149, 7.  
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.