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Yorodumi- EMDB-42024: CryoEM structure of the Drosophila melanogaster flight muscle myo... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-42024 | |||||||||
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Title | CryoEM structure of the Drosophila melanogaster flight muscle myosin filament | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Striated muscle / regulatory protein / myosin / flightin / myofilin / stretchin / STRUCTURAL PROTEIN | |||||||||
Function / homology | Function and homology information myosin ATPase / oscillatory muscle contraction / adult somatic muscle development / striated muscle myosin thick filament assembly / striated muscle myosin thick filament / structural molecule activity conferring elasticity / skeletal muscle myosin thick filament assembly / myosin complex / A band / sarcomere organization ...myosin ATPase / oscillatory muscle contraction / adult somatic muscle development / striated muscle myosin thick filament assembly / striated muscle myosin thick filament / structural molecule activity conferring elasticity / skeletal muscle myosin thick filament assembly / myosin complex / A band / sarcomere organization / structural constituent of muscle / cytoskeletal motor activity / isomerase activity / sarcomere / actin filament binding / ATP binding Similarity search - Function | |||||||||
Biological species | Drosophila melanogaster (fruit fly) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.7 Å | |||||||||
Authors | Abbasi Yeganeh F / Rastegarpouyani H / Li J / Taylor KA | |||||||||
Funding support | United States, 2 items
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Citation | Journal: Int J Mol Sci / Year: 2023 Title: Structure of the Flight Muscle Myosin Filament at 4.7 Å Resolution Reveals New Details of Non-Myosin Proteins. Authors: Fatemeh Abbasi Yeganeh / Hosna Rastegarpouyani / Jiawei Li / Kenneth A Taylor / Abstract: Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain ...Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain comprising its catalytic and actin-binding activities and a long α-helical, coiled tail that forms the dense filament backbone. Myosin alone polymerizes into filaments of irregular length, but striated muscle thick filaments have defined lengths that, with thin filaments, define the sarcomere structure. The motor domain structure and function are well understood, but the myosin filament backbone is not. Here we report on the structure of the flight muscle thick filaments from at 4.7 Å resolution, which eliminates previous ambiguities in non-myosin densities. The full proximal S2 region is resolved, as are the connecting densities between the Ig domains of stretchin-klp. The proteins, flightin, and myofilin are resolved in sufficient detail to build an atomic model based on an AlphaFold prediction. Our results suggest a method by which flightin and myofilin cooperate to define the structure of the thick filament and explains a key myosin mutation that affects flightin incorporation. is a genetic model organism for which our results can define strategies for functional testing. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_42024.map.gz | 1.6 GB | EMDB map data format | |
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Header (meta data) | emd-42024-v30.xml emd-42024.xml | 19.8 KB 19.8 KB | Display Display | EMDB header |
Images | emd_42024.png | 149.3 KB | ||
Filedesc metadata | emd-42024.cif.gz | 6.1 KB | ||
Others | emd_42024_additional_1.map.gz emd_42024_additional_2.map.gz emd_42024_half_map_1.map.gz emd_42024_half_map_2.map.gz | 609.4 KB 31.8 KB 1.2 GB 1.2 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42024 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42024 | HTTPS FTP |
-Related structure data
Related structure data | 8u8hMC 8u95MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_42024.map.gz / Format: CCP4 / Size: 1.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.33 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_42024_additional_1.map | ||||||||||||
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Density Histograms |
-Additional map: #2
File | emd_42024_additional_2.map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_42024_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
File | emd_42024_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Drosophila melanogaster flight muscle thick filament
Entire | Name: Drosophila melanogaster flight muscle thick filament |
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Components |
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-Supramolecule #1: Drosophila melanogaster flight muscle thick filament
Supramolecule | Name: Drosophila melanogaster flight muscle thick filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
-Macromolecule #1: Flightin
Macromolecule | Name: Flightin / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Sequence | String: MADEEDPWGF DDGGEEEKAA STQAGTPAPP SKAPSVASDH KADSVVAGTP ANEEAAPEEV EEIKAPPPP PEDDGYRKPV QLYRHWVRPK FLQYKYMYNY RTNYYDDVID YIDKKQTGVA R EIPRPQTW AERVLRTRNI SGSDIDSYAP AKRDKQLIQT LAASIRTYNY HTKAYINQRY AS VL |
-Macromolecule #2: Myosin
Macromolecule | Name: Myosin / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Sequence | String: MPKPVANQED EDPTPYLFVS LEQRRIDQSK PYDSKKSCWI PDEKEGYLLG EIKATKGDIV SVGLQGGEV RDIKSEKVEK VNPPKFEKIE DMADMTVLNT PCVLHNLRQR YYAKLIYTYS G LFCVAINP YKRYPVYTNR CAKMYRGKRR NEVPPHIFAI SDGAYVDMLT ...String: MPKPVANQED EDPTPYLFVS LEQRRIDQSK PYDSKKSCWI PDEKEGYLLG EIKATKGDIV SVGLQGGEV RDIKSEKVEK VNPPKFEKIE DMADMTVLNT PCVLHNLRQR YYAKLIYTYS G LFCVAINP YKRYPVYTNR CAKMYRGKRR NEVPPHIFAI SDGAYVDMLT NHVNQSMLIT GE SGAGKTE NTKKVIAYFA TVGASKKTDE AAKSKGSLED QVVQTNPVLE AFGNAKTVRN DNS SRFGKF IRIHFGPTGK LAGADIETYL LEKARVISQQ SLERSYHIFY QIMSGSVPGV KDIC LLTDN IYDYHIVSQG KVTVASIDDA EEFSLTDQAF DILGFTKQEK EDVYRITAAV MHMGG MKFK QRGREEQAEQ DGEEEGGRVS KLFGCDTAEL YKNLLKPRIK VGNEFVTQGR NVQQVT NSI GALCKGVFDR LFKWLVKKCN ETLDTQQKRQ HFIGVLDIAG FEIFEYNGFE QLCINFT NE KLQQFFNHIM FVMEQEEYKK EGINWDFIDF GMDLLACIDL IEKPMGILSI LEEESMFP K ATDQTFSEKL TNTHLGKSAP FQKPKPPKPG QQAAHFAIAH YAGCVSYNIT GWLEKNKDP LNDTVVDQFK KSQNKLLIEI FADHAGQSGG GEQAKGGRGK KGGGFATVSS AYKEQLNSLM TTLRSTQPH FVRCIIPNEM KQPGVVDAHL VMHQLTCNGV LEGIRICRKG FPNRMMYPDF K MRYQILNP RGIKDLDCPK KASKVLIEST ELNEDLYRLG HTKVFFRAGV LGQMEEFRDE RL GKIMSWM QAWARGYLSR KGFKKLQEQR VALKVVQRNL RKYLQLRTWP WYKLWQKVKP LLN VSRIED EIARLEEKAK KAEELHAAEV KVRKELEALN AKLLAEKTAL LDSLSGEKGA LQDY QERNA KLTAQKNDLE NQLRDIQERL TQEEDARNQL FQQKKKADQE ISGLKKDIED LELNV QKAE QDKATKDHQI RNLNDEIAHQ DELINKLNKE KKMQGETNQK TGEELQAAED KINHLN KVK AKLEQTLDEL EDSLEREKKV RGDVEKSKRK VEGDLKLTQE AVADLERNKK ELEQTIQ RK DKELSSITAK LEDEQVVVLK HQRQIKELQA RIEELEEEVE AERQARAKAE KQRADLAR E LEELGERLEE AGGATSAQIE LNKKREAELS KLRRDLEEAN IQHESTLANL RKKHNDAVA EMAEQVDQLN KLKAKAEHDR QTCHNELNQT RTACDQLGRD KAAQEKIAKQ LQHTLNEVQS KLDETNRTL NDFDASKKKL SIENSDLLRQ LEEAESQVSQ LSKIKISLTT QLEDTKRLAD E ESRERATL LGKFRNLEHD LDNLREQVEE EAEGKADLQR QLSKANAEAQ VWRSKYESDG VA RSEELEE AKRKLQARLA EAEETIESLN QKCIGLEKTK QRLSTEVEDL QLEVDRANAI ANA AEKKQK AFDKIIGEWK LKVDDLAAEL DASQKECRNY STELFRLKGA YEEGQEQLEA VRRE NKNLA DEVKDLLDQI GEGGRNIHEI EKARKRLEAE KDELQAALEE AEAALEQEEN KVLRA QLEL SQVRQEIDRR IQEKEEEFEN TRKNHQRALD SMQASLEAEA KGKAEALRMK KKLEAD INE LEIALDHANK ANAEAQKNIK RYQQQLKDIQ TALEEEQRAR DDAREQLGIS ERRANAL QN ELEESRTLLE QADRGRRQAE QELADAHEQL NEVSAQNASI SAAKRKLESE LQTLHSDL D ELLNEAKNSE EKAKKAMVDA ARLADELRAE QDHAQTQEKL RKALEQQIKE LQVRLDEAE ANALKGGKKA IQKLEQRVRE LENELDGEQR RHADAQKNLR KSERRVKELS FQSEEDRKNH ERMQDLVDK LQQKIKTYKR QIEEAEEIAA LNLAKFRKAQ QELEEAEERA DLAEQAISKF R AKGRAGSV GRGASPAPRA TSVRPQFDGL AFPPRFDLAP ENEF |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 6.8 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Particle selection | Number selected: 138000 |
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Startup model | Type of model: OTHER / Details: ab-initio model |
Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: PROJECTION MATCHING |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.7 Å / Resolution method: OTHER / Number images used: 116000 |