3I5I

The crystal structure of squid myosin S1 in the presence of SO4 2-


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.330 
  • R-Value Work: 0.262 

wwPDB Validation   3D Report Full Report


This is version 1.2 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
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin heavy chain isoform A839Doryteuthis pealeiiMutation(s): 0 
UniProt
Find proteins for O44934 (Doryteuthis pealeii)
Explore O44934 
Go to UniProtKB:  O44934
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO44934
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin regulatory light chain LC-2, mantle muscle153Todarodes pacificusMutation(s): 0 
UniProt
Find proteins for P08052 (Todarodes pacificus)
Explore P08052 
Go to UniProtKB:  P08052
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08052
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin catalytic light chain LC-1, mantle muscle159Todarodes pacificusMutation(s): 0 
UniProt
Find proteins for P05945 (Todarodes pacificus)
Explore P05945 
Go to UniProtKB:  P05945
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP05945
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.330 
  • R-Value Work: 0.262 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 195.192α = 90
b = 100.153β = 105.45
c = 80.189γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-07-28
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description