2W49

ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions

Wu, S.Liu, J.Reedy, M.C.Tregear, R.T.Winkler, H.Franzini-Armstrong, C.Sasaki, H.Lucaveche, C.Goldman, Y.E.Reedy, M.K.Taylor, K.A.

(2010) PLoS One 5: 12643

  • DOI: https://doi.org/10.1371/journal.pone.0012643
  • Primary Citation of Related Structures:  
    2W49, 2W4A, 2W4G, 2W4T

  • PubMed Abstract: 

    Isometric muscle contraction, where force is generated without muscle shortening, is a molecular traffic jam in which the number of actin-attached motors is maximized and all states of motor action are trapped with consequently high heterogeneity. This heterogeneity is a major limitation to deciphering myosin conformational changes in situ.


  • Organizational Affiliation

    Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, United States of America.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TROPONIN C, SKELETAL MUSCLEA [auth 0],
D [auth 3],
G [auth 6],
J [auth 9]
159Gallus gallusMutation(s): 0 
UniProt
Find proteins for P02588 (Gallus gallus)
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Entity Groups  
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UniProt GroupP02588
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
TROPONIN T, FAST SKELETAL MUSCLE ISOFORMSB [auth 1],
E [auth 4],
H [auth 7],
IA [auth Y]
90Gallus gallusMutation(s): 0 
UniProt
Find proteins for P12620 (Gallus gallus)
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UniProt GroupP12620
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
TROPONIN I, FAST SKELETAL MUSCLEC [auth 2],
F [auth 5],
I [auth 8],
JA [auth Z]
141Gallus gallusMutation(s): 0 
UniProt
Find proteins for P68246 (Gallus gallus)
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UniProt GroupP68246
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
TROPOMYOSIN ALPHA-1 CHAIN277Oryctolagus cuniculusMutation(s): 0 
UniProt
Find proteins for P58772 (Oryctolagus cuniculus)
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UniProt GroupP58772
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
ACTIN, ALPHA SKELETAL MUSCLE372Oryctolagus cuniculusMutation(s): 0 
UniProt
Find proteins for P68135 (Oryctolagus cuniculus)
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UniProt GroupP68135
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CA
Query on CA

Download Ideal Coordinates CCD File 
KA [auth 0]
LA [auth 0]
MA [auth 0]
NA [auth 0]
OA [auth 3]
KA [auth 0],
LA [auth 0],
MA [auth 0],
NA [auth 0],
OA [auth 3],
PA [auth 3],
QA [auth 3],
RA [auth 3],
SA [auth 6],
TA [auth 6],
UA [auth 6],
VA [auth 6],
WA [auth 9],
XA [auth 9],
YA [auth 9],
ZA [auth 9]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIMOD
RECONSTRUCTIONPROTOMO

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-05
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-08-23
    Changes: Data collection
  • Version 1.4: 2019-10-23
    Changes: Data collection, Other