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PDBsum entry 2ff6
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protein ligands metals Protein-protein interface(s) links
Structural protein/contractile protein PDB id
2ff6

 

 

 

 

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Contents
Protein chains
125 a.a. *
11 a.a. *
360 a.a. *
Ligands
ATP
Metals
_CA ×3
Waters ×277
* Residue conservation analysis
PDB id:
2ff6
Name: Structural protein/contractile protein
Title: Crystal structure of gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin
Structure: Gelsolin. Chain: g. Fragment: gelsolin domain 1. Synonym: actin-depolymerizing factor, adf, brevin, agel. Engineered: yes. Cg4944-pc, isoform c. Chain: h. Fragment: ciboulot domain 2. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Oryctolagus cuniculus.
Biol. unit: Trimer (from PQS)
Resolution:
2.05Å     R-factor:   0.204     R-free:   0.237
Authors: A.H.Aguda,B.Xue,R.C.Robinson
Key ref:
A.H.Aguda et al. (2006). The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure, 14, 469-476. PubMed id: 16531231 DOI: 10.1016/j.str.2005.12.011
Date:
19-Dec-05     Release date:   21-Mar-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06396  (GELS_HUMAN) -  Gelsolin from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		782 a.a.
125 a.a.
Protein chain
Pfam   ArchSchema ?
Q8IRS7  (Q8IRS7_DROME) -  Ciboulot, isoform C from Drosophila melanogaster
Seq:
Struc: 		97 a.a.
11 a.a.
Protein chain
Pfam   ArchSchema ?
P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus
Seq:
Struc: 		377 a.a.
360 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.6.4.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.str.2005.12.011 Structure 14:469-476 (2006)
PubMed id: 16531231  
 
 
The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins.
A.H.Aguda, B.Xue, E.Irobi, T.Préat, R.C.Robinson.
 
  ABSTRACT  
 
Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/beta-thymosin (betaT) domain. WH2/betaT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the betaT and WH2 motifs are not functionally analogous.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Comparison of Actin Bound WH2/Tβ Domain Superimposed Structures
(A) The WH2/Tβ chains are shown as Cα traces, and the actin protomer is shown as a ribbon representation (light blue). Cib2 is drawn in light green, Tβ4 (Irobi et al., 2004) is drawn in pink, Cib1 (Hertzog et al., 2004) is drawn in purple, and N-WASP is drawn in black.
(B) A 90° rotation of (A) around the vertical axis.
(C) Comparison of the actin structures from G1-Cib23:actin (blue) and G1-Nw2 (yellow) through superposition of subdomain 4. 		Figure 6.
Figure 6. Schematic Models of the Mechanism of F-Actin Interaction with Tβ Proteins When Bound to More Than One Actin Monomer
(A) Possible interactions with TTβ (black) and actobindin (Act, purple). G-actin and F-actin protomers are depicted in green and light blue, respectively.
(B) Possible interactions of ciboulot (Cib, yellow) with actin. In this mechanism, at the barbed end of the filament (+), the N-terminal helices are proposed to be released by the actin G- to –F-actin transition, while, at the pointed end (−), the C-terminal cap is unaffected by the state of actin. Red crosses signify capped filaments (Irobi et al., 2004).
 
  The above figures are reprinted by permission from Cell Press: Structure (2006, 14, 469-476) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20538977 A.M.Ducka, P.Joel, G.M.Popowicz, K.M.Trybus, M.Schleicher, A.A.Noegel, R.Huber, T.A.Holak, and T.Sitar (2010).
Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.
  Proc Natl Acad Sci U S A, 107, 11757-11762.
PDB codes: 3mmv 3mn5 3mn6 3mn7 3mn9
20536449 C.Husson, F.X.Cantrelle, P.Roblin, D.Didry, K.H.Le, J.Perez, E.Guittet, C.Van Heijenoort, L.Renault, and M.F.Carlier (2010).
Multifunctionality of the beta-thymosin/WH2 module: G-actin sequestration, actin filament growth, nucleation, and severing.
  Ann N Y Acad Sci, 1194, 44-52.  
20529303 S.Koshikawa, R.Cornette, T.Matsumoto, and T.Miura (2010).
The homolog of Ciboulot in the termite (Hodotermopsis sjostedti): a multimeric beta-thymosin involved in soldier-specific morphogenesis.
  BMC Dev Biol, 10, 63.  
19405116 H.G.Mannherz, and E.Hannappel (2009).
The beta-thymosins: intracellular and extracellular activities of a versatile actin binding protein family.
  Cell Motil Cytoskeleton, 66, 839-851.  
19909017 S.Sribenja, M.Li, S.Wongkham, C.Wongkham, Q.Yao, and C.Chen (2009).
Advances in thymosin beta10 research: differential expression, molecular mechanisms, and clinical implications in cancer and other conditions.
  Cancer Invest, 27, 1016-1022.  
18725959 P.M.Medina, R.J.Worthen, L.J.Forsberg, and J.E.Brenman (2008).
The actin-binding protein capulet genetically interacts with the microtubule motor kinesin to maintain neuronal dendrite homeostasis.
  PLoS ONE, 3, e3054.  
17468228 B.Xue, A.H.Aguda, and R.C.Robinson (2007).
Models of the actin-bound forms of the beta-thymosins.
  Ann N Y Acad Sci, 1112, 56-66.  
18042452 M.Bosch, K.H.Le, B.Bugyi, J.J.Correia, L.Renault, and M.F.Carlier (2007).
Analysis of the function of Spire in actin assembly and its synergy with formin and profilin.
  Mol Cell, 28, 555-568.  
17947587 M.F.Carlier, M.Hertzog, D.Didry, L.Renault, F.X.Cantrelle, C.van Heijenoort, M.Knossow, and E.Guittet (2007).
Structure, function, and evolution of the beta-thymosin/WH2 (WASP-Homology2) actin-binding module.
  Ann N Y Acad Sci, 1112, 67-75.  
17526584 X.Zheng, K.Diraviyam, and D.Sept (2007).
Nucleotide effects on the structure and dynamics of actin.
  Biophys J, 93, 1277-1283.  
16731556 R.B.Dickinson, and D.L.Purich (2006).
Diffusion rate limitations in actin-based propulsion of hard and deformable particles.
  Biophys J, 91, 1548-1563.  
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.

 

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