+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-22145 | ||||||||||||
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Title | 10S myosin II (smooth muscle) | ||||||||||||
Map data | 10S myosin II (smooth muscle) | ||||||||||||
Sample |
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Keywords | motor protein / auto-inhibited form / 10 S conformation / CONTRACTILE PROTEIN | ||||||||||||
Function / homology | Function and homology information myofibril assembly / myosin filament / actomyosin structure organization / myosin II complex / structural constituent of muscle / microfilament motor activity / myofibril / stress fiber / platelet aggregation / actin filament binding ...myofibril assembly / myosin filament / actomyosin structure organization / myosin II complex / structural constituent of muscle / microfilament motor activity / myofibril / stress fiber / platelet aggregation / actin filament binding / calcium ion binding / ATP binding / cytosol Similarity search - Function | ||||||||||||
Biological species | Meleagris gallopavo (turkey) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||||||||
Authors | Yang S / Craig R | ||||||||||||
Funding support | United States, 3 items
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Citation | Journal: Nature / Year: 2020 Title: Cryo-EM structure of the inhibited (10S) form of myosin II. Authors: Shixin Yang / Prince Tiwari / Kyoung Hwan Lee / Osamu Sato / Mitsuo Ikebe / Raúl Padrón / Roger Craig / Abstract: Myosin II is the motor protein that enables muscle cells to contract and nonmuscle cells to move and change shape. The molecule has two identical heads attached to an elongated tail, and can exist in ...Myosin II is the motor protein that enables muscle cells to contract and nonmuscle cells to move and change shape. The molecule has two identical heads attached to an elongated tail, and can exist in two conformations: 10S and 6S, named for their sedimentation coefficients. The 6S conformation has an extended tail and assembles into polymeric filaments, which pull on actin filaments to generate force and motion. In 10S myosin, the tail is folded into three segments and the heads bend back and interact with each other and the tail, creating a compact conformation in which ATPase activity, actin activation and filament assembly are all highly inhibited. This switched-off structure appears to function as a key energy-conserving storage molecule in muscle and nonmuscle cells, which can be activated to form functional filaments as needed-but the mechanism of its inhibition is not understood. Here we have solved the structure of smooth muscle 10S myosin by cryo-electron microscopy with sufficient resolution to enable improved understanding of the function of the head and tail regions of the molecule and of the key intramolecular contacts that cause inhibition. Our results suggest an atomic model for the off state of myosin II, for its activation and unfolding by phosphorylation, and for understanding the clustering of disease-causing mutations near sites of intramolecular interaction. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_22145.map.gz | 6 MB | EMDB map data format | |
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Header (meta data) | emd-22145-v30.xml emd-22145.xml | 23.8 KB 23.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_22145_fsc.xml | 10.7 KB | Display | FSC data file |
Images | emd_22145.png | 121.5 KB | ||
Filedesc metadata | emd-22145.cif.gz | 7.7 KB | ||
Others | emd_22145_half_map_1.map.gz emd_22145_half_map_2.map.gz | 80.8 MB 80.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-22145 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-22145 | HTTPS FTP |
-Validation report
Summary document | emd_22145_validation.pdf.gz | 723.4 KB | Display | EMDB validaton report |
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Full document | emd_22145_full_validation.pdf.gz | 723 KB | Display | |
Data in XML | emd_22145_validation.xml.gz | 17.4 KB | Display | |
Data in CIF | emd_22145_validation.cif.gz | 22.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22145 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-22145 | HTTPS FTP |
-Related structure data
Related structure data | 6xe9MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_22145.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | 10S myosin II (smooth muscle) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.328 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: 10S myosin II (smooth muscle) half map
File | emd_22145_half_map_1.map | ||||||||||||
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Annotation | 10S myosin II (smooth muscle) half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: 10S myosin II (smooth muscle) half map
File | emd_22145_half_map_2.map | ||||||||||||
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Annotation | 10S myosin II (smooth muscle) half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Smooth muscle myosin II
Entire | Name: Smooth muscle myosin II |
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Components |
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-Supramolecule #1: Smooth muscle myosin II
Supramolecule | Name: Smooth muscle myosin II / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Whole myosin II isolated from turkey gizzard |
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Source (natural) | Organism: Meleagris gallopavo (turkey) / Organ: gizzard / Tissue: smooth muscle |
Molecular weight | Theoretical: 530 KDa |
-Macromolecule #1: Myosin II heavy chain (smooth muscle)
Macromolecule | Name: Myosin II heavy chain (smooth muscle) / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: myosin ATPase |
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Source (natural) | Organism: Meleagris gallopavo (turkey) |
Molecular weight | Theoretical: 229.14825 KDa |
Sequence | String: MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE LQENGKKVTL SKDDIQKMNP PKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL FCVVVNPYKQ LPIYSEKIID MYKGKKRHEM PPHIYAIADT A YRSMLQDR ...String: MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE LQENGKKVTL SKDDIQKMNP PKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL FCVVVNPYKQ LPIYSEKIID MYKGKKRHEM PPHIYAIADT A YRSMLQDR EDQSILCTGE SGAGKTENTK KVIQYLAVVA SSHKGKKDTS ITQGPSFSYG ELEKQLLQAN PILEAFGNAK TV KNDNSSR FGKFIRINFD VTGYIVGANI ETYLLEKSRA IRQAKDERTF HIFYYLIAGA SEQMRNDLLL EGFNNYTFLS NGH VPIPAQ QDDEMFQETL EAMRIMGFTE EEQTSILRVV SSVLQLGNIV FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTR SILTP RIKVGRDVVQ KAQTKEQADF AIEALAKAKF ERLFRWILTR VNKALDKTKR QGASFLGILD IAGFEIFEIN SFEQL CINY TNEKLQQLFN HTMFILEQEE YQREGIEWNF IDFGLDLQPC IELIERPTNP PGVLALLDEE CWFPKATDTS FVEKLI QEQ GNHPKFQKSK QLKDKTEFCI LHYAGKVSYN ASAWLTKNMD PLNDNVTSLL NQSSDKFVAD LWKDVDRIVG LDQMAKM TE SSLPSSSKTK KGMFRTVGQL YKEQLTKLMT TLRNTNPNFV RCIIPNHEKR AGKLDAHLVL EQLRCNGVLE GIRICRQG F PNRIVFQEFR QRYEILAANA IPKGFMDGKQ ACILMIKALE LDPNLYRIGQ SKIFFRTGVL AHLEEERDLK ITDVIIAFQ AQCRGYLARK AFAKRQQQLT AMKVIQRNCA AYLKLRNWQW WRLFTKVKPL LQVTRQEEEM QAKDEELQRT KERQQKAEAE LKELEQKHT QLCEEKNLLQ EKLQAETELY AEAEEMRVRL AAKKQELEEI LHEMEARIEE EEERSQQLQA EKKKMQQQML D LEEQLEEE EAARQKLQLE KVTADGKIKK MEDDILIMED QNNKLTKERK LLEERVSDLT TNLAEEEEKA KNLTKLKNKH ES MISELEV RLKKEEKTRQ ELEKTKRKLE GESSDLHEQI AELQAQIAEL KAQLAKKEEE LQAALARLED ETSQKNNALK KIR ELESHI SDLQEDLESE KAARNKAEKQ KRDLGEELEA LKTELEDTLD TTATQQELRA KREQEVTVLK RALEEETRTH EAQV QEMRQ KHTQAVEELT EQLEQFKRAK ANLDKTKQTL EKDNADLANE VRSLSQAKQD VEHKKKKLEV QLQDLQSKYT DGERV RTEL NEKVHKLQIE VENVTSLLNE AESKNIKLTK DVATLGSQLQ DTQELLQEET RQKLNVTTKL RQLEDDKNSL QEQLDE EVE AKQNLERHIS TLTIQLSDSK KKLQEFTATI ETMEEGKKKF QREIESLTQQ FEEKAASYDK LEKTKNRLQQ ELDDLVV DL DNQRQLVSNL EKKQKKFDQM LAEEKNISSK YADERDRAEA EAREKETKAL SLARALEEAL EAKEELERTN KMLKAEME D LVSSKDDVGK NVHELEKSKR TLEQQVEEMK TQLEELEDEL QAAEDAKLRL EVNMQAMKSQ FERDLQARDE QNEEKRRQL LKQLHEHETE LEDERKQRAL AAAAKKKLEV DVKDLESQVD SVNKAREEAI KQLRKLQAQM KDYQRDLDDA RAAREEIFAT ARENEKKAK NLEAELIQLQ EDLAAAERAR KQADLEKEEM AEELASATSG RTSLQDDKRR LEARIAQLEE ELDEEHSNIE A MSDRMRKA VQQAEQLNNE LATERATAQK NENARQQLER QNKELRSKLQ EMEGAVKSKF KSTIAALEAK IASLEEQLEQ EA REKQAAA KTLRQKDKKL KDALLQVEDE KKQAEQYKDQ AEKGNLRLKQ LKRQLEEAEE ESQRINANRR KLQRELDEAT ESN DALGRE VAALKSKLRR GNEPVSFAPP RRSGGRRVIE NATDGGEQEI DGRDGDLNGK ASE |
-Macromolecule #2: Myosin light chain smooth muscle isoform
Macromolecule | Name: Myosin light chain smooth muscle isoform / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Meleagris gallopavo (turkey) |
Molecular weight | Theoretical: 16.989145 KDa |
Sequence | String: MCDFSEEQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVMK VLGNPKSDEM NLKTLNFEQF LPMMQTIAKN KDQGCFEDY VEGLRVFDKE GNGTVMGAEI RHVLVTLGEK MTEEEVEQLV AGHEDSNGCI NYEELVRMVL SG UniProtKB: Myosin light chain smooth muscle isoform |
-Macromolecule #3: Myosin light chain 9
Macromolecule | Name: Myosin light chain 9 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Meleagris gallopavo (turkey) |
Molecular weight | Theoretical: 19.872244 KDa |
Sequence | String: MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS MGKNPTDEYL EGMMSEAPGP INFTMFLTM FGEKLNGTDP EDVIRNAFAC FDEEASGFIH EDHLRELLTT MGDRFTDEEV DEMYREAPID KKGNFNYVEF T RILKHGAK DKDD UniProtKB: EF-hand domain-containing protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.1 mg/mL | ||||||||||||||||||
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Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR | ||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV | ||||||||||||||||||
Details | The specimen was cross-linked in presence of 0.1% glutaraldehyde for 60 seconds. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 10951 / Average electron dose: 43.3 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |