1DFL

SCALLOP MYOSIN S1 COMPLEXED WITH MGADP:VANADATE-TRANSITION STATE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å
  • R-Value Free: 0.400 
  • R-Value Work: 0.394 
  • R-Value Observed: 0.394 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Three conformational states of scallop myosin S1.

Houdusse, A.Szent-Gyorgyi, A.G.Cohen, C.

(2000) Proc Natl Acad Sci U S A 97: 11238-11243

  • DOI: https://doi.org/10.1073/pnas.200376897
  • Primary Citation of Related Structures:  
    1DFK, 1DFL

  • PubMed Abstract: 

    We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free state and in the presence of MgADP.V04, corresponding to the transition state. These two new structures, together with the previously determined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reveal three conformations of an intact S1 obtained from a single isoform. These studies, together with new crystallization results, show how the conformation of the motor depends on the nucleotide content of the active site. The resolution of the two new structures ( approximately 4 A) is sufficient to establish the relative positions of the subdomains and the overall conformation of the joints within the motor domain as well as the position of the lever arm. Comparison of available crystal structures from different myosin isoforms and truncated constructs in either the nucleotide-free or transition states indicates that the major features within the motor domain are relatively invariant in both these states. In contrast, the position of the lever arm varies significantly between different isoforms. These results indicate that the heavy-chain helix is pliant at the junction between the converter and the lever arm and that factors other than the precise position of the converter can influence the position of the lever arm. It is possible that this pliant junction in the myosin head contributes to the compliance known to be present in the crossbridge.


  • Organizational Affiliation

    Rosenstiel Basic Medical Sciences Research Center, and Biology Department, Brandeis University, Waltham, MA 02254-9110, USA. Anne.Houdusse@curie.fr


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MYOSIN HEADA,
D [auth B]
831Argopecten irradiansMutation(s): 0 
UniProt
Find proteins for P24733 (Argopecten irradians)
Explore P24733 
Go to UniProtKB:  P24733
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24733
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MYOSIN HEADB [auth Y],
E [auth W]
139Argopecten irradiansMutation(s): 0 
UniProt
Find proteins for P13543 (Argopecten irradians)
Explore P13543 
Go to UniProtKB:  P13543
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP13543
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
MYOSIN HEADC [auth Z],
F [auth X]
152Argopecten irradiansMutation(s): 0 
UniProt
Find proteins for P07291 (Argopecten irradians)
Explore P07291 
Go to UniProtKB:  P07291
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07291
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ADP
Query on ADP

Download Ideal Coordinates CCD File 
I [auth A],
N [auth B]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
VO4
Query on VO4

Download Ideal Coordinates CCD File 
H [auth A],
M [auth B]
VANADATE ION
O4 V
LSGOVYNHVSXFFJ-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
K [auth Z],
P [auth X]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
G [auth A],
J [auth Y],
L [auth B],
O [auth W]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å
  • R-Value Free: 0.400 
  • R-Value Work: 0.394 
  • R-Value Observed: 0.394 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.032α = 90
b = 243.475β = 100.2
c = 124.65γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-10-25
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-31
    Changes: Experimental preparation
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations