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PDBsum entry 2v52

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protein ligands metals Protein-protein interface(s) links
Structural protein/contractile protein PDB id
2v52

 

 

 

 

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Contents
Protein chains
360 a.a.
30 a.a. *
Ligands
LAB
ATP
GOL ×2
Metals
_MG
Waters ×359
* Residue conservation analysis
PDB id:
2v52
Name: Structural protein/contractile protein
Title: Structure of mal-rpel2 complexed to g-actin
Structure: Actin, alpha skeletal muscle. Chain: b. Synonym: actin, alpha skeletal muscle, alpha-actin-1. Mkl/myocardin-like protein 1. Chain: m. Fragment: rpel2. Synonym: mrtf-a, mal, megakaryoblastic leukemia 1 protein homolog, basic sap coiled-coil transcription activator. Engineered: yes
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Synthetic: yes. Mus musculus. Mouse. Organism_taxid: 10090
Resolution:
1.45Å     R-factor:   0.149     R-free:   0.188
Authors: S.Mouilleron,S.Guettler,C.A.Langer,R.Treisman,N.Q.Mcdonald
Key ref: S.Mouilleron et al. (2008). Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. Embo J, 27, 3198-3208. PubMed id: 19008859
Date:
01-Oct-08     Release date:   25-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus
Seq:
Struc:
377 a.a.
360 a.a.
Protein chain
Pfam   ArchSchema ?
Q8K4J6  (MKL1_MOUSE) -  Myocardin-related transcription factor A from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
964 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: Chain B: E.C.3.6.4.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chain M: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
Embo J 27:3198-3208 (2008)
PubMed id: 19008859  
 
 
Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.
S.Mouilleron, S.Guettler, C.A.Langer, R.Treisman, N.Q.McDonald.
 
  ABSTRACT  
 
Serum response factor transcriptional activity is controlled through interactions with regulatory cofactors such as the coactivator MAL/MRTF-A (myocardin-related transcription factor A). MAL is itself regulated in vivo by changes in cellular actin dynamics, which alter its interaction with G-actin. The G-actin-sensing mechanism of MAL/MRTF-A resides in its N-terminal domain, which consists of three tandem RPEL repeats. We describe the first molecular insights into RPEL function obtained from structures of two independent RPEL(MAL) peptide:G-actin complexes. Both RPEL peptides bind to the G-actin hydrophobic cleft and to subdomain 3. These RPEL(MAL):G-actin structures explain the sequence conservation defining the RPEL motif, including the invariant arginine. Characterisation of the RPEL(MAL):G-actin interaction by fluorescence anisotropy and cell reporter-based assays validates the significance of actin-binding residues for proper MAL localisation and regulation in vivo. We identify important differences in G-actin engagement between the two RPEL(MAL) structures. Comparison with other actin-binding proteins reveals an unexpected similarity to the vitamin-D-binding protein, extending the G-actin-binding protein repertoire.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20088824 B.Visegrády, and L.M.Machesky (2010).
Myopathy-causing actin mutations promote defects in serum-response factor signalling.
  Biochem J, 427, 41-48.  
20414257 E.N.Olson, and A.Nordheim (2010).
Linking actin dynamics and gene transcription to drive cellular motile functions.
  Nat Rev Mol Cell Biol, 11, 353-365.  
20687691 K.Amano, T.Yoshidome, M.Iwaki, M.Suzuki, and M.Kinoshita (2010).
Entropic potential field formed for a linear-motor protein near a filament: Statistical-mechanical analyses using simple models.
  J Chem Phys, 133, 045103.  
20877641 L.Jin, Q.Gan, B.J.Zieba, S.M.Goicoechea, G.K.Owens, C.A.Otey, and A.V.Somlyo (2010).
The actin associated protein palladin is important for the early smooth muscle cell differentiation.
  PLoS One, 5, e12823.  
20236507 L.Leitner, D.Shaposhnikov, A.Descot, R.Hoffmann, and G.Posern (2010).
Epithelial Protein Lost in Neoplasm alpha (Eplin-alpha) is transcriptionally regulated by G-actin and MAL/MRTF coactivators.
  Mol Cancer, 9, 60.  
20071339 M.W.Chan, F.Chaudary, W.Lee, J.W.Copeland, and C.A.McCulloch (2010).
Force-induced myofibroblast differentiation through collagen receptors is dependent on mammalian diaphanous (mDia).
  J Biol Chem, 285, 9273-9281.  
20818336 R.Pawłowski, E.K.Rajakylä, M.K.Vartiainen, and R.Treisman (2010).
An actin-regulated importin α/β-dependent extended bipartite NLS directs nuclear import of MRTF-A.
  EMBO J, 29, 3448-3458.  
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.

 

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