2OS8

Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.27 Å
  • R-Value Free: 0.314 
  • R-Value Work: 0.281 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor.

Yang, Y.Gourinath, S.Kovacs, M.Nyitray, L.Reutzel, R.Himmel, D.M.O'neall-Hennessey, E.Reshetnikova, L.Szent-Gyorgyi, A.G.Brown, J.H.Cohen, C.

(2007) Structure 15: 553-564

  • DOI: https://doi.org/10.1016/j.str.2007.03.010
  • Primary Citation of Related Structures:  
    2EC6, 2OS8, 2OTG, 3I5F, 3I5G, 3I5H, 3I5I

  • PubMed Abstract: 

    Unlike processive cellular motors such as myosin V, whose structure has recently been determined in a "rigor-like" conformation, myosin II from contracting muscle filaments necessarily spends most of its time detached from actin. By using squid and sea scallop sources, however, we have now obtained similar rigor-like atomic structures for muscle myosin heads (S1). The significance of the hallmark closed actin-binding cleft in these crystal structures is supported here by actin/S1-binding studies. These structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of detailed differences in interdomain contacts. Moreover, the rigor-like position of switch II turns out to be unique for myosin V. The overall arrangements of subdomains in the motor are relatively conserved in each of the known contractile states, and we explore qualitatively the energetics of these states.


  • Organizational Affiliation

    Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin heavy chain840Placopecten magellanicusMutation(s): 0 
UniProt
Find proteins for Q26080 (Placopecten magellanicus)
Explore Q26080 
Go to UniProtKB:  Q26080
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UniProt GroupQ26080
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin regulatory light chain157Placopecten magellanicusMutation(s): 0 
UniProt
Find proteins for Q26068 (Placopecten magellanicus)
Explore Q26068 
Go to UniProtKB:  Q26068
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UniProt GroupQ26068
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin essential light chain157Placopecten magellanicusMutation(s): 0 
UniProt
Find proteins for Q26066 (Placopecten magellanicus)
Explore Q26066 
Go to UniProtKB:  Q26066
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ26066
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.27 Å
  • R-Value Free: 0.314 
  • R-Value Work: 0.281 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.567α = 90
b = 50.359β = 98.72
c = 161.621γ = 90
Software Package:
Software NamePurpose
CNSrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-05-29
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description