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- PDB-6so3: The interacting head motif in insect flight muscle myosin thick f... -

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Basic information

Entry
Database: PDB / ID: 6so3
TitleThe interacting head motif in insect flight muscle myosin thick filaments
Components
  • Myosin 2 essential light chain striated muscle
  • Myosin 2 heavy chain striated muscle
  • Myosin 2 regulatory light chain striated muscle
KeywordsMOTOR PROTEIN / myosin / thick filament / insect flight muscle
Biological speciesLethocerus indicus (insect)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 6.2 Å
AuthorsMorris, E.P. / Knupp, C. / Squire, J.M.
CitationJournal: Biology (Basel) / Year: 2019
Title: The Interacting Head Motif Structure Does Not Explain the X-Ray Diffraction Patterns in Relaxed Vertebrate (Bony Fish) Skeletal Muscle and Insect () Flight Muscle.
Authors: Carlo Knupp / Edward Morris / John M Squire /
Abstract: Unlike electron microscopy, which can achieve very high resolution but to date can only be used to study static structures, time-resolved X-ray diffraction from contracting muscles can, in principle, ...Unlike electron microscopy, which can achieve very high resolution but to date can only be used to study static structures, time-resolved X-ray diffraction from contracting muscles can, in principle, be used to follow the molecular movements involved in force generation on a millisecond timescale, albeit at moderate resolution. However, previous X-ray diffraction studies of resting muscles have come up with structures for the head arrangements in resting myosin filaments that are different from the apparently ubiquitous interacting head motif (IHM) structures found by single particle analysis of electron micrographs of isolated myosin filaments from a variety of muscle types. This head organization is supposed to represent the super-relaxed state of the myosin filaments where adenosine triphosphate (ATP) usage is minimized. Here we have tested whether the interacting head motif structures will satisfactorily explain the observed low-angle X-ray diffraction patterns from resting vertebrate (bony fish) and invertebrate (insect flight) muscles. We find that the interacting head motif does not, in fact, explain what is observed. Previous X-ray models fit the observations much better. We conclude that the X-ray diffraction evidence has been well interpreted in the past and that there is more than one ordered myosin head state in resting muscle. There is, therefore, no reason to question some of the previous X-ray diffraction results on myosin filaments; time-resolved X-ray diffraction should be a reliable way to follow crossbridge action in active muscle and may be one of the few ways to visualise the molecular changes in myosin heads on a millisecond timescale as force is actually produced.
History
DepositionAug 28, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 8, 2020Provider: repository / Type: Initial release

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Structure visualization

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Assembly

Deposited unit
B: Myosin 2 heavy chain striated muscle
D: Myosin 2 essential light chain striated muscle
F: Myosin 2 regulatory light chain striated muscle
A: Myosin 2 heavy chain striated muscle
C: Myosin 2 essential light chain striated muscle
E: Myosin 2 regulatory light chain striated muscle


Theoretical massNumber of molelcules
Total (without water)527,9296
Polymers527,9296
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area32650 Å2
ΔGint-121 kcal/mol
Surface area77740 Å2
MethodPISA

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Components

#1: Protein Myosin 2 heavy chain striated muscle


Mass: 224542.281 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lethocerus indicus (insect)
#2: Protein Myosin 2 essential light chain striated muscle


Mass: 17628.104 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lethocerus indicus (insect)
#3: Protein Myosin 2 regulatory light chain striated muscle


Mass: 21794.281 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Lethocerus indicus (insect)

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Myosin thick filament / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Lethocerus indicus (insect)
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Specimen holderCryogen: NITROGEN
Image recordingElectron dose: 65 e/Å2 / Film or detector model: DIRECT ELECTRON DE-20 (5k x 3k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 33.98 ° / Axial rise/subunit: 145 Å / Axial symmetry: C4
3D reconstructionResolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24000 / Symmetry type: HELICAL

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