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PDBsum entry 3dtp

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protein Protein-protein interface(s) links
Contractile protein PDB id
3dtp
Jmol
Contents
Protein chains
938 a.a. *
148 a.a. *
196 a.a. *
* Residue conservation analysis
PDB id:
3dtp
Name: Contractile protein
Title: Tarantula heavy meromyosin obtained by flexible docking to tarantula muscle thick filament cryo-em 3d-map
Structure: Myosin 2 heavy chain chimera of smooth and cardiac muscle. Chain: a. Fragment: subfragment 1(s1), delta-s2 (residues 2-972). Synonym: myosin heavy chain, gizzard smooth muscle, cardiac muscle beta isoform, myhc-beta, myosin heavy chain slow isoform, myhc-slow. Engineered: yes. Myosin 2 heavy chain chimera of smooth and
Source: Gallus gallus, homo sapiens. Chicken, human. Organism_taxid: 9031,9606. Expressed in: spodoptera frugiperda, escherichia coli. Expression_system_taxid: 7108,511693. Expression_system_cell_line: sf9. Gallus gallus. Chicken. Expressed in: spodoptera frugiperda.
Authors: L.Alamo,W.Wriggers,A.Pinto,F.Bartoli,L.Salazar,F.Q.Zhao, R.Craig,R.Padron
Key ref:
L.Alamo et al. (2008). Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. J Mol Biol, 384, 780-797. PubMed id: 18951904 DOI: 10.1016/j.jmb.2008.10.013
Date:
15-Jul-08     Release date:   07-Oct-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10587  (MYH11_CHICK) -  Myosin-11
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1979 a.a.
938 a.a.*
Protein chains
Pfam   ArchSchema ?
P12883  (MYH7_HUMAN) -  Myosin-7
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1935 a.a.
938 a.a.*
Protein chains
Pfam   ArchSchema ?
P02607  (MYL6_CHICK) -  Myosin light polypeptide 6
Seq:
Struc:
151 a.a.
148 a.a.
Protein chains
Pfam   ArchSchema ?
B4XT43  (B4XT43_9ARAC) -  Myosin II regulatory light chain
Seq:
Struc:
196 a.a.
196 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure
* PDB and UniProt seqs differ at 479 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytosol   5 terms 
  Biological process     actomyosin structure organization   2 terms 
  Biochemical function     protein binding     7 terms  

 

 
DOI no: 10.1016/j.jmb.2008.10.013 J Mol Biol 384:780-797 (2008)
PubMed id: 18951904  
 
 
Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.
L.Alamo, W.Wriggers, A.Pinto, F.Bártoli, L.Salazar, F.Q.Zhao, R.Craig, R.Padrón.
 
  ABSTRACT  
 
Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in addition to those seen previously. To help interpret the interactions, we sequenced the tarantula RLC and fitted an atomic model of the myosin head that included the predicted RLC atomic structure and an S2 (subfragment 2) crystal structure to the reconstruction. The fitting suggests one intramolecular interaction, between the cardiomyopathy loop of the free head and its own S2, and two intermolecular interactions, between the cardiac loop of the free head and the essential light chain of the blocked head and between the Leu305-Gln327 interaction loop of the free head and the N-terminal fragment of the RLC of the blocked head. These interactions, added to those previously described, would help switch off the thick filament. Molecular dynamics simulations suggest how phosphorylation could increase the helical content of the RLC N-terminus, weakening these interactions, thus releasing both heads and activating the thick filament.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. Predicted atomic structure for the tarantula RLC obtained using the PredictProtein server.^33 The structure has three domains: domain 1 (helices A–D), domain 2 (helices E–H), and domain 3 (helices L and P). The predicted secondary structure for the 52-aa NTF (domain 3 or “phosphorylation domain“^13) is formed by the positively charged helices L and P (with phosphorylatable Ser35 and Ser45) connected by a Pro–Ala coil linker. The 8.5-nm IQ motif helix of the myosin heavy chain (Glu812–Phe855) is shown in light gray.
Figure 8.
Fig. 8. Five of the reported mutations in the myosin head heavy chain and S2 associated with familial hypertrophic CM. Myosin heavy chain: R403Q, R403L, or R403W (orange sphere) in the CM loop (yellow) and E924K (grey spheres), E927K (pink spheres), E930K (cyan spheres), and E935K (yellow spheres) in the negatively charged ring 2 of S2,^45 facing the CM loop. The side-chain orientations at the interface of the loop may be unreliable as this is not a structure determination down to atomic detail but a prediction at an amino acid level of detail. See the legend to Fig. 6b.
 
  The above figures are reprinted from an Open Access publication published by Elsevier: J Mol Biol (2008, 384, 780-797) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21419133 H.S.Jung, N.Billington, K.Thirumurugan, B.Salzameda, C.R.Cremo, J.M.Chalovich, P.D.Chantler, and P.J.Knight (2011).
Role of the tail in the regulated state of myosin 2.
  J Mol Biol, 408, 863-878.  
21177429 O.Pylypenko, and A.M.Houdusse (2011).
Essential "ankle" in the myosin lever arm.
  Proc Natl Acad Sci U S A, 108, 5-6.  
21504733 P.Hooijman, M.A.Stewart, and R.Cooke (2011).
A new state of cardiac myosin with very slow ATP turnover: a potential cardioprotective mechanism in the heart.
  Biophys J, 100, 1969-1976.  
21516138 R.Cooke (2011).
The role of the myosin ATPase activity in adaptive thermogenesis by skeletal muscle.
  Biophys Rev, 3, 33-45.  
20404208 D.Kast, L.M.Espinoza-Fonseca, C.Yi, and D.D.Thomas (2010).
Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain.
  Proc Natl Acad Sci U S A, 107, 8207-8212.  
19966283 M.A.Stewart, K.Franks-Skiba, S.Chen, and R.Cooke (2010).
Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers.
  Proc Natl Acad Sci U S A, 107, 430-435.  
20174447 W.Wriggers (2010).
Using Situs for the integration of multi-resolution structures.
  Biophys Rev, 2, 21-27.  
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.