8EW5

The structure of flightin within myosin thick filaments from Bombus ignitus flight muscle


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.00 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of the Flight Muscle Thick Filament from the Bumble Bee, Bombus ignitus , at 6 angstrom Resolution.

Li, J.Rahmani, H.Abbasi Yeganeh, F.Rastegarpouyani, H.Taylor, D.W.Wood, N.B.Previs, M.J.Iwamoto, H.Taylor, K.A.

(2022) Int J Mol Sci 24

  • DOI: https://doi.org/10.3390/ijms24010377
  • Primary Citation of Related Structures:  
    8EW5

  • PubMed Abstract: 

    Four insect orders have flight muscles that are both asynchronous and indirect; they are asynchronous in that the wingbeat frequency is decoupled from the frequency of nervous stimulation and indirect in that the muscles attach to the thoracic exoskeleton instead of directly to the wing. Flight muscle thick filaments from two orders, Hemiptera and Diptera, have been imaged at a subnanometer resolution, both of which revealed a myosin tail arrangement referred to as “curved molecular crystalline layers”. Here, we report a thick filament structure from the indirect flight muscles of a third insect order, Hymenoptera, the Asian bumble bee Bombus ignitus. The myosin tails are in general agreement with previous determinations from Lethocerus indicus and Drosophila melanogaster. The Skip 2 region has the same unusual structure as found in Lethocerus indicus thick filaments, an α-helix discontinuity is also seen at Skip 4, but the orientation of the Skip 1 region on the surface of the backbone is less angled with respect to the filament axis than in the other two species. The heads are disordered as in Drosophila, but we observe no non-myosin proteins on the backbone surface that might prohibit the ordering of myosin heads onto the thick filament backbone. There are strong structural similarities among the three species in their non-myosin proteins within the backbone that suggest how one previously unassigned density in Lethocerus might be assigned. Overall, the structure conforms to the previously observed pattern of high similarity in the myosin tail arrangement, but differences in the non-myosin proteins.


  • Organizational Affiliation

    Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Flightin152Bombus ignitusMutation(s): 0 
UniProt
Find proteins for A0A6J3L7M6 (Bombus vosnesenskii)
Explore A0A6J3L7M6 
Go to UniProtKB:  A0A6J3L7M6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A6J3L7M6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.00 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Japan Society for the Promotion of Science (JSPS)Japan19K06777
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR01 GM030598
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR35 GM139616
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)United StatesR21 AR077802
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)United StatesR01 HL157487
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesU24 GM116788
American Heart AssociationUnited States20PRE35120273

Revision History  (Full details and data files)

  • Version 1.0: 2023-01-04
    Type: Initial release
  • Version 1.1: 2023-01-18
    Changes: Database references