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- EMDB-20084: The Central Role of the Tail in Switching Off Myosin II in Cells -

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Basic information

Entry
Database: EMDB / ID: EMD-20084
TitleThe Central Role of the Tail in Switching Off Myosin II in Cells
Map data3D reconstruction of smooth muscle myosin II molecule in the inhibited state
Sample
  • Organelle or cellular component: Myosin IIMyosin
    • Other: Myosin IIMyosin
KeywordsSmooth Muscle / MyosinII / 10S / single particle analysis / CONTRACTILE PROTEIN
Biological speciesMeleagris gallopavo (turkey)
Methodsingle particle reconstruction / negative staining / Resolution: 25.0 Å
AuthorsCraig R / Yang SX / Lee KH / Woodhead JL / Sato O / Ikebe M
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin DiseasesR01AR067279 United States
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin DiseasesR01AR072036 United States
National Institutes of Health/National Heart, Lung, and Blood InstituteR01HL139883 United States
CitationJournal: J Gen Physiol / Year: 2019
Title: The central role of the tail in switching off 10S myosin II activity.
Authors: Shixin Yang / Kyoung Hwan Lee / John L Woodhead / Osamu Sato / Mitsuo Ikebe / Roger Craig /
Abstract: Myosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. ...Myosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. Its inactive form is a monomer with a compact structure (10S sedimentation coefficient), in which the tail is folded and the two heads interact with each other, inhibiting activity. This conformation is thought to function in cells as an energy-conserving form of the molecule suitable for storage as well as transport to sites of filament assembly. The mechanism of inhibition of the compact molecule is not fully understood. We have performed a 3-D reconstruction of negatively stained 10S myosin from smooth muscle in the inhibited state using single-particle analysis. The reconstruction reveals multiple interactions between the tail and the two heads that appear to trap ATP hydrolysis products, block actin binding, hinder head phosphorylation, and prevent filament formation. Blocking these essential features of myosin function could explain the high degree of inhibition of the folded form of myosin thought to underlie its energy-conserving function in cells. The reconstruction also suggests a mechanism for unfolding when myosin is activated by phosphorylation.
History
DepositionApr 10, 2019-
Header (metadata) releaseApr 24, 2019-
Map releaseApr 24, 2019-
UpdateSep 6, 2023-
Current statusSep 6, 2023Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20084.png

Downloads & links

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Map

FileDownload / File: emd_20084.map.gz / Format: CCP4 / Size: 12.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation3D reconstruction of smooth muscle myosin II molecule in the inhibited state
Voxel sizeX=Y=Z: 3.7 Å
Density
Contour LevelBy AUTHOR: 0.015 / Movie #1: 0.015
Minimum - Maximum-0.03206814 - 0.115241796
Average (Standard dev.)0.0000618078 (±0.0036309515)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions150150150
Spacing150150150
CellA=B=C: 555.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z3.73.73.7
M x/y/z150150150
origin x/y/z0.0000.0000.000
length x/y/z555.000555.000555.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS150150150
D min/max/mean-0.0320.1150.000

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Supplemental data

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Sample components

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Entire : Myosin II

EntireName: Myosin IIMyosin
Components
  • Organelle or cellular component: Myosin IIMyosin
    • Other: Myosin IIMyosin

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Supramolecule #1: Myosin II

SupramoleculeName: Myosin II / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Meleagris gallopavo (turkey)

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Macromolecule #1: Myosin II

MacromoleculeName: Myosin II / type: other / ID: 1 / Classification: other
Source (natural)Organism: Meleagris gallopavo (turkey)
SequenceString: MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE LQENGKKVT LSKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL F CVVINPYK QLPIYSEKII DMYKGKKRHE MPPHIYAIAD TAYRSMLQDR ...String:
MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE LQENGKKVT LSKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL F CVVINPYK QLPIYSEKII DMYKGKKRHE MPPHIYAIAD TAYRSMLQDR EDQSILCTGE SG AGKTENT KKVIQYLAVV ASSHKGKKDT SITQGPSFSY GELEKQLLQA NPILEAFGNA KTV KNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQAKDERT FHIFYYLIAG ASEQ MRNDL LLEGFNNYTF LSNGHVPIPA QQDDEMFQET LEAMTIMGFT EEEQTSILRV VSSVL QLGN IVFKKERNTD QASMPDNTAA QKVCHLMGIN VTDFTRSILT PRIKVGRDVV QKAQTK EQA DFAIEALAKA KFERLFRWIL TRVNKALDKT KRQGASFLGI LDIAGFEIFE INSFEQL CI NYTNEKLQQL FNHTMFILEQ EEYQREGIEW NFIDFGLDLQ PCIELIERPT NPPGVLAL L DEECWFPKAT DTSFVEKLIQ EQGNHAKFQK SKQLKDKTEF CILHYAGKVT YNASAWLTK NMDPLNDNVT SLLNQSSDKF VADLWKDVDR IVGLDQMAKM TESSLPSASK TKKGMFRTVG QLYKEQLTK LMTTLRNTNP NFVRCIIPNH EKRAGKLDAH LVLEQLRCNG VLEGIRICRQ G FPNRIVFQ EFRQRYEILA ANAIPKGFMD GKQACILMIK ALELDPNLYR IGQSKIFFRT GV LAHLEEE RDLKITDVII AFQAQCRGYL ARKAFAKRQQ QLTAMKVIQR NCAAYLKLRN WQW WRLFTK VKPLLQVTRQ EEEMQAKDEE LQRTKERQQK AEAELKELEQ KHTQLCEEKN LLQE KLQAE TELYAEAEEM RVRLAAKKQE LEEILHEMEA RIEEEEERSQ QLQAEKKKMQ QQMLD LEEQ LEEEEAARQK LQLEKVTADG KIKKMEDDIL IMEDQNNKLT KERKLLEERV SDLTTN LAE EEEKAKNLTK LKNKHESMIS ELEVRLKKEE KSRQELEKIK RKLEGESSDL HEQIAEL QA QIAELKAQLA KKEEELQAAL ARLEDETSQK NNALKKIREL ESHISDLQED LESEKAAR N KAEKQKRDLS EELEALKTEL EDTLDTTATQ QELRAKREQE VTVLKRALEE ETRTHEAQV QEMRQKHTQA VEELTEQLEQ FKRAKANLDK TKQTLEKDNA DLANEIRSLS QAKQDVEHKK KKLEVQLQD LQSKYSDGER VRTELNEKVH KLQIEVENVT SLLNEAESKN IKLTKDVATL G SQLQDTQE LLQEETRQKL NVTTKLRQLE DDKNSLQEQL DEEVEAKQNL ERHISTLTIQ LS DSKKKLQ EFTATVETME EGKKKLQREI ESLTQQFEEK AASYDKLEKT KNRLQQELDD LVV DLDNQR QLVSNLEKKQ KKFDQMLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEE ALEAK EELERTNKML KAEMEDLVSS KDDVGKNVHE LEKSKRTLEQ QVEEMKTQLE ELEDE LQAA EDAKLRLEVN MQAMKSQFER DLQARDEQNE EKRRQLLKQL HEHETELEDE RKQRAL AAA AKKKLEVDVK DLESQVDSAN KAREEAIKQL RKLQAQMKDY QRDLDDARAA REEIFAT AR ENEKKAKNLE AELIQLQEDL AAAERARKQA DLEKEEMAEE LASANSGRTS LQDEKRRL E ARIAQLEEEL DEEHSNIETM SDRMRKAVQQ AEQLNNELAT ERATAQKNEN ARQQLERQN KELRSKLQEM EGAVKSKFKS TIAALEAKIA SLEEQLEQEA REKQAAAKTL RQKDKKLKDA LLQVEDERK QAEQYKDQAE KGNLRLKQLK RQLEEAEEES QRINANRRKL QRELDEATES N DALGREVA ALKSKLRRGN EPVSFAPPRR SGGRRVIENA TDGGEEEIDG RDGDFNGKAS E

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Experimental details

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Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
StainingType: NEGATIVE / Material: uranyl acetate
GridDetails: unspecified

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Electron microscopy

MicroscopeFEI/PHILIPS CM120T
Electron beamAcceleration voltage: 120 kV / Electron source: LAB6
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: TVIPS TEMCAM-F224 (2k x 2k) / Average electron dose: 20.0 e/Å2

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Image processing

Startup modelType of model: RANDOM CONICAL TILT
Initial angle assignmentType: OTHER
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionResolution.type: BY AUTHOR / Resolution: 25.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 15833

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