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- EMDB-13521: Cryo-EM structure of the actomyosin-V complex in the strong-ADP s... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-13521 | ||||||||||||||||||
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Title | Cryo-EM structure of the actomyosin-V complex in the strong-ADP state (central 1er) | ||||||||||||||||||
![]() | Sharpened map of the central actomyosin-V-LC molecule filtered to local resolution | ||||||||||||||||||
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Function / homology | ![]() minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / muscle myosin complex / muscle filament sliding / vesicle transport along actin filament / myosin II complex / myosin complex / structural constituent of muscle / cytoskeletal motor activator activity ...minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / muscle myosin complex / muscle filament sliding / vesicle transport along actin filament / myosin II complex / myosin complex / structural constituent of muscle / cytoskeletal motor activator activity / microfilament motor activity / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / filamentous actin / cytoskeletal motor activity / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / Smooth Muscle Contraction / skeletal muscle fiber development / muscle contraction / stress fiber / skeletal muscle tissue development / titin binding / vesicle-mediated transport / actin filament polymerization / filopodium / protein localization to plasma membrane / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cellular response to insulin stimulus / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / lamellipodium / cell body / vesicle / calmodulin binding / hydrolase activity / protein domain specific binding / Golgi membrane / calcium ion binding / positive regulation of gene expression / magnesium ion binding / extracellular exosome / ATP binding / identical protein binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||||||||
![]() | Pospich S / Sweeney HL / Houdusse A / Raunser S | ||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Authors: Sabrina Pospich / H Lee Sweeney / Anne Houdusse / Stefan Raunser / ![]() ![]() ![]() Abstract: The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are ...The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin. | ||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 25.9 KB 25.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.7 KB | Display | ![]() |
Images | ![]() | 98.8 KB | ||
Masks | ![]() | 125 MB | ![]() | |
Others | ![]() ![]() ![]() ![]() | 1.5 MB 12.1 MB 59.1 MB 59 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7pm5MC ![]() 7pltC ![]() 7pluC ![]() 7plvC ![]() 7plwC ![]() 7plxC ![]() 7plyC ![]() 7plzC ![]() 7pm0C ![]() 7pm1C ![]() 7pm2C ![]() 7pm3C ![]() 7pm6C ![]() 7pm7C ![]() 7pm8C ![]() 7pm9C ![]() 7pmaC ![]() 7pmbC ![]() 7pmcC ![]() 7pmdC ![]() 7pmeC ![]() 7pmfC ![]() 7pmgC ![]() 7pmhC ![]() 7pmiC ![]() 7pmjC ![]() 7pmlC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Sharpened map of the central actomyosin-V-LC molecule filtered to local resolution | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: Sharpened map of the central actomyosin-V-LC molecule filtered...
File | emd_13521_additional_1.map | ||||||||||||
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Annotation | Sharpened map of the central actomyosin-V-LC molecule filtered to nominal resolution | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Denoised map of the central actomyosin-V-LC molecule (LAFTER)
File | emd_13521_additional_2.map | ||||||||||||
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Annotation | Denoised map of the central actomyosin-V-LC molecule (LAFTER) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map (signal subtracted particles)
File | emd_13521_half_map_1.map | ||||||||||||
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Annotation | Half map (signal subtracted particles) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map (signal subtracted particles)
File | emd_13521_half_map_2.map | ||||||||||||
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Annotation | Half map (signal subtracted particles) | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Actomyosin-V complex in the strong-ADP state
Entire | Name: Actomyosin-V complex in the strong-ADP state |
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Components |
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-Supramolecule #1: Actomyosin-V complex in the strong-ADP state
Supramolecule | Name: Actomyosin-V complex in the strong-ADP state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 Details: Aged ADP-bound F-actin stabilized with phalloidin and decorated with myosin-Va-LC in the strong-ADP state (Mg2+-ADP) |
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-Macromolecule #1: Myosin light chain 6B
Macromolecule | Name: Myosin light chain 6B / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 17.090277 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MIEFNKDQLE EFKEAFELFD RVGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEL KSRRVDFETF LPMLQAVAKN RGQGTYEDY LEGFRVFDKE GNGKVMGAEL RHVLTTLGEK MTEEEVETVL AGHEDSNGCI NYEAFLKHIL SV |
-Macromolecule #2: Unconventional myosin-Va
Macromolecule | Name: Unconventional myosin-Va / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 91.363953 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAASELYTKY ARVWIPDPEE VWKSAELLKD YKPGDKVLQL RLEEGKDLEY CLDPKTKELP PLRNPDILVG ENDLTALSYL HEPAVLHNL KVRFIDSKLI YTYCGIVLVA INPYEQLPIY GEDIINAYSG QNMGDMDPHI FAVAEEAYKQ MARDERNQSI I VSGESGAG ...String: MAASELYTKY ARVWIPDPEE VWKSAELLKD YKPGDKVLQL RLEEGKDLEY CLDPKTKELP PLRNPDILVG ENDLTALSYL HEPAVLHNL KVRFIDSKLI YTYCGIVLVA INPYEQLPIY GEDIINAYSG QNMGDMDPHI FAVAEEAYKQ MARDERNQSI I VSGESGAG KTVSAKYAMR YFATVSGSAS EANVEEKVLA SNPIMESIGN AKTTRNDNSS RFGKYIEIGF DKRYRIIGAN MR TYLLEKS RVVFQAEEER NYHIFYQLCA SAALPEFKTL RLGNANYFHY TKQGGSPVID GIDDAKEMVN TRQACTLLGI SDS YQMGIF RILAGILHLG NVEFASRDSD SCAIPPKHDP LTIFCDLMGV DYEEMAHWLC HRKLATATET YIKPISKLHA INAR DALAK HIYANLFNWI VDHVNKALHS TVKQHSFIGV LDIYGFETFE INSFEQFCIN YANEKLQQQF NMHVFKLEQE EYMKE QIPW TLIDFYDNQP CINLIEAKMG VLDLLDEECK MPKGSDDTWA QKLYNTHLNK CALFEKPRLS NKAFIIKHFA DKVEYQ CEG FLEKNKDTVY EEQIKVLKSS KKFKLLPELF QDEEKAISPT SATPSGRVPL SRTPVKPAKA RPGQTSKEHK KTVGHQF RN SLHLLMETLN ATTPHYVRCI KPNDFKFPFT FDEKRAVQQL RACGVLETIR ISAAGFPSRW TYQEFFSRYR VLMKQKDV L SDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK IRADKLRAAC IRIQKTIRGW LMRKKYMRMR R |
-Macromolecule #3: Actin, alpha skeletal muscle
Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 42.109973 KDa |
Sequence | String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY ...String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSS S LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQ KEITALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F |
-Macromolecule #4: Phalloidin
Macromolecule | Name: Phalloidin / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 808.899 Da |
Sequence | String: W(EEP)A(DTH)C(HYP)A |
-Macromolecule #5: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 2 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 286 K / Instrument: FEI VITROBOT MARK III / Details: On grid decoration. |
Details | Rise 27.8 A, Twist -167.3 degrees |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Number grids imaged: 1 / Number real images: 5908 / Average exposure time: 15.0 sec. / Average electron dose: 82.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |