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- EMDB-29646: Acto-HMM complex in ADP-state. Chicken smooth muscle HMM and chic... -

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Basic information

Entry
Database: EMDB / ID: EMD-29646
TitleActo-HMM complex in ADP-state. Chicken smooth muscle HMM and chicken pectoralis actin
Map dataTwo-headed attachment - Post-classification - filtered map
Sample
  • Complex: Acto-HMM complex - chicken smooth muscle heavy meromyosin in complex with chicken pectoralis muscle actin filament
    • Protein or peptide: Myosin regulatory light chain 2, smooth muscle major isoform
    • Protein or peptide: Myosin-11
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Myosin light polypeptide 6
KeywordsActin / Myosin / Smooth muscle / Cryo-EM / Cryo-ET / Heavy meromyosin / MOTOR PROTEIN
Function / homology
Function and homology information


RHO GTPases activate PAKs / myosin II filament / Smooth Muscle Contraction / myofibril assembly / elastic fiber assembly / myosin light chain binding / skeletal muscle myosin thick filament assembly / muscle myosin complex / myosin II binding / Striated Muscle Contraction ...RHO GTPases activate PAKs / myosin II filament / Smooth Muscle Contraction / myofibril assembly / elastic fiber assembly / myosin light chain binding / skeletal muscle myosin thick filament assembly / muscle myosin complex / myosin II binding / Striated Muscle Contraction / actomyosin / myosin filament / actomyosin structure organization / myosin II complex / cardiac muscle cell development / myosin complex / structural constituent of muscle / microfilament motor activity / myofibril / myosin heavy chain binding / skeletal muscle thin filament assembly / cytoskeletal motor activity / striated muscle thin filament / smooth muscle contraction / skeletal muscle fiber development / stress fiber / actin filament / ADP binding / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / actin filament binding / actin binding / calmodulin binding / hydrolase activity / calcium ion binding / magnesium ion binding / ATP binding / cytosol / cytoplasm
Similarity search - Function
DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin head, motor domain / Myosin head (motor domain) ...DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / IQ motif profile. / IQ motif, EF-hand binding site / Actins signature 1. / Actin, conserved site / Actins signature 2. / Kinesin motor domain superfamily / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / EF-hand domain pair / EF-hand, calcium binding motif / ATPase, nucleotide binding domain / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Myosin, heavy chain 11, smooth muscle / Myosin light polypeptide 6 / Myosin regulatory light chain 2, smooth muscle major isoform / Myosin-11 / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesGallus gallus (chicken)
Methodsingle particle reconstruction / cryo EM / Resolution: 19.0 Å
AuthorsHojjatian A / Liu J / Taylor DW / Daneshparvar N / Trybus KM / Taylor KA
Funding support United States, 9 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)R01 AR47421 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)r01 gm30598 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM139616 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM136288 United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)S10 RR11357 United States
National Science Foundation (NSF, United States)BIR-9512954 United States
National Institutes of Health/Office of the DirectorS10 OD018142 United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)S10 RR025080 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM116788 United States
CitationJournal: J Struct Biol / Year: 2023
Title: Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.
Authors: Alimohammad Hojjatian / Dianne W Taylor / Nadia Daneshparvar / Patricia M Fagnant / Kathleen M Trybus / Kenneth A Taylor /
Abstract: Force production in muscle is achieved through the interaction of myosin and actin. Strong binding states in active muscle are associated with Mg·ADP bound to the active site; release of Mg·ADP ...Force production in muscle is achieved through the interaction of myosin and actin. Strong binding states in active muscle are associated with Mg·ADP bound to the active site; release of Mg·ADP allows rebinding of ATP and dissociation from actin. Thus, Mg·ADP binding is positioned for adaptation as a force sensor. Mechanical loads on the lever arm can affect the ability of myosin to release Mg·ADP but exactly how this is done is poorly defined. Here we use F-actin decorated with double-headed smooth muscle myosin fragments in the presence of Mg·ADP to visualize the effect of internally supplied tension on the paired lever arms using cryoEM. The interaction of the paired heads with two adjacent actin subunits is predicted to place one lever arm under positive and the other under negative strain. The converter domain is believed to be the most flexible domain within myosin head. Our results, instead, point to the segment of heavy chain between the essential and regulatory light chains as the location of the largest structural change. Moreover, our results suggest no large changes in the myosin coiled coil tail as the locus of strain relief when both heads bind F-actin. The method would be adaptable to double-headed members of the myosin family. We anticipate that the study of actin-myosin interaction using double-headed fragments enables visualization of domains that are typically noisy in decoration with single-headed fragments.
History
DepositionJan 31, 2023-
Header (metadata) releaseAug 30, 2023-
Map releaseAug 30, 2023-
UpdateAug 30, 2023-
Current statusAug 30, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_29646.png

Downloads & links

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Map

FileDownload / File: emd_29646.map.gz / Format: CCP4 / Size: 35.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTwo-headed attachment - Post-classification - filtered map
Voxel sizeX=Y=Z: 2.56 Å
Density
Contour LevelBy AUTHOR: 0.0472
Minimum - Maximum-0.12679195 - 0.26061592
Average (Standard dev.)0.000246139 (±0.026049202)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions210210210
Spacing210210210
CellA=B=C: 537.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Acto-HMM - Pre-classification - filtered map

Fileemd_29646_additional_1.map
AnnotationActo-HMM - Pre-classification - filtered map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Two-headed attachment - Post-classification - unfiltered half map 1

Fileemd_29646_half_map_1.map
AnnotationTwo-headed attachment - Post-classification - unfiltered half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Two-headed attachment - Post-classification - unfiltered half map 2

Fileemd_29646_half_map_2.map
AnnotationTwo-headed attachment - Post-classification - unfiltered half map 2
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Acto-HMM complex - chicken smooth muscle heavy meromyosin in comp...

EntireName: Acto-HMM complex - chicken smooth muscle heavy meromyosin in complex with chicken pectoralis muscle actin filament
Components
  • Complex: Acto-HMM complex - chicken smooth muscle heavy meromyosin in complex with chicken pectoralis muscle actin filament
    • Protein or peptide: Myosin regulatory light chain 2, smooth muscle major isoform
    • Protein or peptide: Myosin-11
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Myosin light polypeptide 6

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Supramolecule #1: Acto-HMM complex - chicken smooth muscle heavy meromyosin in comp...

SupramoleculeName: Acto-HMM complex - chicken smooth muscle heavy meromyosin in complex with chicken pectoralis muscle actin filament
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Gallus gallus (chicken)

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Macromolecule #1: Myosin regulatory light chain 2, smooth muscle major isoform

MacromoleculeName: Myosin regulatory light chain 2, smooth muscle major isoform
type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Gallus gallus (chicken)
Molecular weightTheoretical: 16.583412 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
FDQSQIQEFK EAFNMIDQNR DGFIDKEDLH DMLASMGKNP TDEYLEGMMS EAPGPINFTM FLTMFGEKLN GTDPEDVIRN AFACFDEEA SGFIHEDHLR ELLTTMGDRF TDEEVDEMYR EAPIDKKGNF NYVEFTRILK HGAK

UniProtKB: Myosin regulatory light chain 2, smooth muscle major isoform

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Macromolecule #2: Myosin-11

MacromoleculeName: Myosin-11 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Gallus gallus (chicken)
Molecular weightTheoretical: 97.534883 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: SQKPLSDDEK FLFVDKNFVN NPLAQADWSA KKLVWVPSEK HGFEAASIKE EKGDEVTVEL QENGKKVTLS KDDIQKMNPP KFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA Y RSMLQDRE ...String:
SQKPLSDDEK FLFVDKNFVN NPLAQADWSA KKLVWVPSEK HGFEAASIKE EKGDEVTVEL QENGKKVTLS KDDIQKMNPP KFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA Y RSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAVVAS SHKGKKDTSI TQGPSFSYGE LEKQLLQANP ILEAFGNAKT VK NDNSSRF GKFIRINFDV TGYIVGANIE TYLLEKSRAI RQAKDERTFH IFYYLIAGAS EQMRNDLLLE GFNNYTFLSN GHV PIPAQQ DDEMFQETLE AMTIMGFTEE EQTSILRVVS SVLQLGNIVF KKERNTDQAS MPDNTAAQKV CHLMGINVTD FTRS ILTPR IKVGRDVVQK AQTKEQADFA IEALAKAKFE RLFRWILTRV NKALDKTKRQ GASFLGILDI AGFEIFEINS FEQLC INYT NEKLQQLFNH TMFILEQEEY QREGIEWNFI DFGLDLQPCI ELIERPTNPP GVLALLDEEC WFPKATDTSF VEKLIQ EQG NHAKFQKSKQ LKDKTEFCIL HYAGKVTYNA SAWLTKNMDP LNDNVTSLLN QSSDKFVADL WKDVDRIVGL DQMAKMT ES SLPSASKTKK GMFRTVGQLY KEQLTKLMTT LRNTNPNFVR CIIPNHEKRA GKLDAHLVLE QLRCNGVLEG IRICRQGF P NRIVFQEFRQ RYEILAANAI PKGFMDGKQA CILMIKALEL DPNLYRIGQS KIFFRTGVLA HLEEERDLKI TDVIIAFQA QCRGYLARKA FAKRQQQLTA MKVIQRNCAA YLKLRNWQWW RLFTKVKPLL

UniProtKB: Myosin-11

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Macromolecule #3: Actin, alpha skeletal muscle

MacromoleculeName: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Gallus gallus (chicken)
Molecular weightTheoretical: 41.862613 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIITNWD DMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV T HNVPIYEG ...String:
DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIITNWD DMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV T HNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN VMSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ITKQEYDEAG PSIVHRKCF

UniProtKB: Actin, alpha skeletal muscle

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Macromolecule #4: Myosin light polypeptide 6

MacromoleculeName: Myosin light polypeptide 6 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Gallus gallus (chicken)
Molecular weightTheoretical: 16.639715 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
FSEEQTAEFK EAFQLFDRTG DGKILYSQCG DVMRALGQNP TNAEVMKVLG NPKSDEMNLK TLNFEQFLPM MQTIAKNKDQ GCFEDYVEG LRVFDKEGNG TVMGAEIRHV LVTLGEKMTE EEVEQLVAGH EDSNGCINYE ELVRMVLSG

UniProtKB: Myosin light polypeptide 6

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 20.0 µm / Nominal defocus min: 0.2 µm
Image recordingFilm or detector model: DIRECT ELECTRON DE-64 (8k x 8k) / Detector mode: INTEGRATING / Average electron dose: 29.6 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 19.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 17394
FSC plot (resolution estimation)

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