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PDBsum entry 1yxq

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protein ligands metals Protein-protein interface(s) links
Contractile protein PDB id
1yxq
Jmol
Contents
Protein chains
356 a.a.
Ligands
ATP ×2
EDO ×2
SWI
Metals
_MG ×3
Waters ×282
PDB id:
1yxq
Name: Contractile protein
Title: Crystal structure of actin in complex with swinholide a
Structure: Actin, alpha skeletal muscle. Chain: a, b. Synonym: alpha-actin 1
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986
Resolution:
2.01Å     R-factor:   0.186     R-free:   0.219
Authors: V.A.Klenchin,R.King,J.Tanaka,G.Marriott,I.Rayment
Key ref:
V.A.Klenchin et al. (2005). Structural basis of swinholide A binding to actin. Chem Biol, 12, 287-291. PubMed id: 15797212 DOI: 10.1016/j.chembiol.2005.02.011
Date:
22-Feb-05     Release date:   17-May-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle
Seq:
Struc:
377 a.a.
356 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   5 terms 
  Biological process     skeletal muscle fiber development   2 terms 
  Biochemical function     nucleotide binding     3 terms  

 

 
DOI no: 10.1016/j.chembiol.2005.02.011 Chem Biol 12:287-291 (2005)
PubMed id: 15797212  
 
 
Structural basis of swinholide A binding to actin.
V.A.Klenchin, R.King, J.Tanaka, G.Marriott, I.Rayment.
 
  ABSTRACT  
 
Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. Here we present a 2.0 A resolution structure of swinholide A, a marine macrolide, bound to two actin molecules. The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other. The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization. The observed structure reveals the mechanism of action of swinholide A and provides a structural framework about which to design new agents directed at the cytoskeleton.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure, Electron Density, and Ligand Contacts for the Actin-Swinholide A Complex
Figure 2.
Figure 2. Swinholide A and Kabiramide C Occupy the Same Binding Site on Actin
 
  The above figures are reprinted by permission from Cell Press: Chem Biol (2005, 12, 287-291) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20797609 J.C.Blain, Y.F.Mok, J.Kubanek, and J.S.Allingham (2010).
Two molecules of lobophorolide cooperate to stabilize an actin dimer using both their "ring" and "tail" region.
  Chem Biol, 17, 802-807.
PDB code: 3m6g
18391412 M.R.Sawaya, D.S.Kudryashov, I.Pashkov, H.Adisetiyo, E.Reisler, and T.O.Yeates (2008).
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
  Acta Crystallogr D Biol Crystallogr, 64, 454-465.
PDB codes: 2q1n 2q31 2q36
19008859 S.Mouilleron, S.Guettler, C.A.Langer, R.Treisman, and N.Q.McDonald (2008).
Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.
  EMBO J, 27, 3198-3208.
PDB codes: 2v51 2v52
17351011 J.L.Melville, I.H.Moal, C.Baker-Glenn, P.E.Shaw, G.Pattenden, and J.D.Hirst (2007).
The structural determinants of macrolide-actin binding: in silico insights.
  Biophys J, 92, 3862-3867.  
17268607 J.W.Blunt, B.R.Copp, W.P.Hu, M.H.Munro, P.T.Northcote, and M.R.Prinsep (2007).
Marine natural products.
  Nat Prod Rep, 24, 31-86.  
17573428 M.Böhl, S.Tietze, A.Sokoll, S.Madathil, F.Pfennig, J.Apostolakis, K.Fahmy, and H.O.Gutzeit (2007).
Flavonoids affect actin functions in cytoplasm and nucleus.
  Biophys J, 93, 2767-2780.  
16141336 D.S.Kudryashov, M.R.Sawaya, H.Adisetiyo, T.Norcross, G.Hegyi, E.Reisler, and T.O.Yeates (2005).
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.
  Proc Natl Acad Sci U S A, 102, 13105-13110.
PDB code: 2a5x
16192358 J.S.Allingham, A.Zampella, M.V.D'Auria, and I.Rayment (2005).
Structures of microfilament destabilizing toxins bound to actin provide insight into toxin design and activity.
  Proc Natl Acad Sci U S A, 102, 14527-14532.
PDB codes: 2asm 2aso 2asp
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.