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- EMDB-22067: Bovine Cardiac Myosin in Complex with Chicken Skeletal Actin and ... -

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基本情報

登録情報
データベース: EMDB / ID: EMD-22067
タイトルBovine Cardiac Myosin in Complex with Chicken Skeletal Actin and Human Cardiac Tropomyosin in the Rigor State
マップデータCryo-EM map of the cardiac actin-myosin-tropomyosin complex.
試料
  • 複合体: Helical complex of bovine S1 cardiac myosin and human cardiac tropomyosin-decorated chicken skeletal actin filaments
    • 複合体: S1 cardiac myosin
      • タンパク質・ペプチド: Tropomyosin alpha-1 chain
    • 複合体: cardiac tropomyosin
      • タンパク質・ペプチド: Myosin-7
    • 細胞器官・細胞要素: skeletal actin filaments
      • タンパク質・ペプチド: Actin, alpha skeletal muscle
  • リガンド: ADENOSINE-5'-DIPHOSPHATE
  • リガンド: MAGNESIUM ION
キーワードmyosin / tropomyosin / actin / cardiac / CONTRACTILE PROTEIN
機能・相同性
機能・相同性情報


positive regulation of heart rate by epinephrine / muscle thin filament tropomyosin / bleb / Striated Muscle Contraction / negative regulation of vascular associated smooth muscle cell migration / regulation of muscle contraction / muscle filament sliding / myosin filament / ruffle organization / adult heart development ...positive regulation of heart rate by epinephrine / muscle thin filament tropomyosin / bleb / Striated Muscle Contraction / negative regulation of vascular associated smooth muscle cell migration / regulation of muscle contraction / muscle filament sliding / myosin filament / ruffle organization / adult heart development / positive regulation of ATP-dependent activity / Striated Muscle Contraction / ventricular cardiac muscle tissue morphogenesis / structural constituent of muscle / regulation of heart contraction / myosin II complex / microfilament motor activity / myofibril / sarcomere organization / negative regulation of vascular associated smooth muscle cell proliferation / skeletal muscle thin filament assembly / striated muscle thin filament / positive regulation of cell adhesion / Smooth Muscle Contraction / skeletal muscle fiber development / cardiac muscle contraction / stress fiber / positive regulation of stress fiber assembly / cytoskeleton organization / cytoskeletal protein binding / sarcomere / negative regulation of cell migration / actin filament / actin filament organization / 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 / wound healing / structural constituent of cytoskeleton / ruffle membrane / cellular response to reactive oxygen species / actin filament binding / actin cytoskeleton / actin binding / regulation of cell shape / cytoskeleton / hydrolase activity / calmodulin binding / protein heterodimerization activity / protein homodimerization activity / ATP binding / identical protein binding / cytoplasm / cytosol
類似検索 - 分子機能
Tropomyosins signature. / Tropomyosin / Tropomyosin / 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. ...Tropomyosins signature. / Tropomyosin / Tropomyosin / 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. / 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 / ATPase, nucleotide binding domain / P-loop containing nucleoside triphosphate hydrolase
類似検索 - ドメイン・相同性
Tropomyosin alpha-1 chain / Actin, alpha skeletal muscle / Myosin-7
類似検索 - 構成要素
生物種Bos taurus (ウシ) / Homo sapiens (ヒト) / Gallus gallus (ニワトリ)
手法らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 4.24 Å
データ登録者Doran MH / Lehman W / Bullitt E
資金援助 米国, European Union, 7件
OrganizationGrant number国
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL036153 米国
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL123774 米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)S10RR25434 米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM129541 米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM029090 米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24GM116787 米国
Horizon 2020 Research and Innovation Programme777204 SILICOFCMEuropean Union
引用ジャーナル: Biophys J / 年: 2020
タイトル: Cryo-EM and Molecular Docking Shows Myosin Loop 4 Contacts Actin and Tropomyosin on Thin Filaments.
著者: Matthew H Doran / Elumalai Pavadai / Michael J Rynkiewicz / Jonathan Walklate / Esther Bullitt / Jeffrey R Moore / Michael Regnier / Michael A Geeves / William Lehman /
要旨: The motor protein myosin drives muscle and nonmuscle motility by binding to and moving along actin of thin filaments. Myosin binding to actin also modulates interactions of the regulatory protein, ...The motor protein myosin drives muscle and nonmuscle motility by binding to and moving along actin of thin filaments. Myosin binding to actin also modulates interactions of the regulatory protein, tropomyosin, on thin filaments, and conversely tropomyosin affects myosin binding to actin. Insight into this reciprocity will facilitate a molecular level elucidation of tropomyosin regulation of myosin interaction with actin in muscle contraction, and in turn, promote better understanding of nonmuscle cell motility. Indeed, experimental approaches such as fiber diffraction, cryoelectron microscopy, and three-dimensional reconstruction have long been used to define regulatory interaction of tropomyosin and myosin on actin at a structural level. However, their limited resolution has not proven sufficient to determine tropomyosin and myosin contacts at an atomic-level and thus to fully substantiate possible functional contributions. To overcome this deficiency, we have followed a hybrid approach by performing new cryogenic electron microscopy reconstruction of myosin-S1-decorated F-actin-tropomyosin together with atomic scale protein-protein docking of tropomyosin to the EM models. Here, cryo-EM data were derived from filaments reconstituted with α1-actin, cardiac αα-tropomyosin, and masseter muscle β-myosin complexes; masseter myosin, which shares sequence identity with β-cardiac myosin-heavy chain, was used because of its stability in vitro. The data were used to build an atomic model of the tropomyosin cable that fits onto the actin filament between the tip of the myosin head and a cleft on the innermost edge of actin subunits. The docking and atomic scale fitting showed multiple discrete interactions of myosin loop 4 and acidic residues on successive 39-42 residue-long tropomyosin pseudorepeats. The contacts between S1 and tropomyosin on actin appear to compete with and displace ones normally found between actin and tropomyosin on myosin-free thin filaments in relaxed muscle, thus restructuring the filament during myosin-induced activation.
履歴
登録2020年5月27日-
ヘッダ(付随情報) 公開2020年7月22日-
マップ公開2020年7月22日-
更新2024年3月6日-
現状2024年3月6日処理サイト: RCSB / 状態: 公開

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構造の表示

ムービー
  • 表面図（断面を密度値に従い着色）
  • 表面レベル: 0.01
  • UCSF Chimeraによる作画
  • ダウンロード
  • 表面図（円筒半径に従い着色）
  • 表面レベル: 0.01
  • UCSF Chimeraによる作画
  • ダウンロード
  • あてはめたモデルとの重ね合わせ
  • 原子モデル: PDB-6x5z
  • 表面レベル: 0.01
  • UCSF Chimeraによる作画
  • ダウンロード
  • 単純化した表面モデル + あてはめた原子モデル
  • 原子モデルPDB-6x5z
  • Jmolによる作画
  • ダウンロード
ムービービューア
構造ビューアEMマップ:
SurfViewMolmilJmol/JSmol
添付画像

emd_22067.png

ダウンロードとリンク

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マップ

ファイルダウンロード / ファイル: emd_22067.map.gz / 形式: CCP4 / 大きさ: 64 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈Cryo-EM map of the cardiac actin-myosin-tropomyosin complex.
ボクセルのサイズX=Y=Z: 1.06 Å
密度
表面レベル登録者による: 0.007 / ムービー #1: 0.01
最小 - 最大-0.03484657 - 0.058786064
平均 (標準偏差)0.00039920956 (±0.0025944682)
対称性空間群: 1
詳細

EMDB XML:

マップ形状
Axis orderXYZ
Origin000
サイズ256256256
Spacing256256256
セルA=B=C: 271.36 Å
α=β=γ: 90.0 °

CCP4マップ ヘッダ情報:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z271.360271.360271.360
α/β/γ90.00090.00090.000
start NX/NY/NZ434333
NX/NY/NZ116118137
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.0350.0590.000

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添付データ

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試料の構成要素

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全体 : Helical complex of bovine S1 cardiac myosin and human cardiac tro...

全体名称: Helical complex of bovine S1 cardiac myosin and human cardiac tropomyosin-decorated chicken skeletal actin filaments
要素
  • 複合体: Helical complex of bovine S1 cardiac myosin and human cardiac tropomyosin-decorated chicken skeletal actin filaments
    • 複合体: S1 cardiac myosin
      • タンパク質・ペプチド: Tropomyosin alpha-1 chain
    • 複合体: cardiac tropomyosin
      • タンパク質・ペプチド: Myosin-7
    • 細胞器官・細胞要素: skeletal actin filaments
      • タンパク質・ペプチド: Actin, alpha skeletal muscle
  • リガンド: ADENOSINE-5'-DIPHOSPHATE
  • リガンド: MAGNESIUM ION

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超分子 #1: Helical complex of bovine S1 cardiac myosin and human cardiac tro...

超分子名称: Helical complex of bovine S1 cardiac myosin and human cardiac tropomyosin-decorated chicken skeletal actin filaments
タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#3
詳細: Bovine myosin was isolated from the masseter muscle and the S1 fragment was generated through proteolytic cleavage.
分子量理論値: 403.22 KDa

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超分子 #3: S1 cardiac myosin

超分子名称: S1 cardiac myosin / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #2
由来(天然)生物種: Bos taurus (ウシ) / 組織: Masseter Muscle

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超分子 #4: cardiac tropomyosin

超分子名称: cardiac tropomyosin / タイプ: complex / ID: 4 / 親要素: 1 / 含まれる分子: #3
由来(天然)生物種: Homo sapiens (ヒト)

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超分子 #2: skeletal actin filaments

超分子名称: skeletal actin filaments / タイプ: organelle_or_cellular_component / ID: 2 / 親要素: 1 / 含まれる分子: #1
由来(天然)生物種: Gallus gallus (ニワトリ) / 組織: Breast Skeletal Muscle

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分子 #1: Actin, alpha skeletal muscle

分子名称: Actin, alpha skeletal muscle / タイプ: protein_or_peptide / ID: 1
詳細: Residues 1-9 and 377 were disordered and were not modeled.
コピー数: 3 / 光学異性体: LEVO
由来(天然)生物種: Gallus gallus (ニワトリ) / 組織: Breast Skeletal Muscle
分子量理論値: 42.096953 KDa
配列文字列: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHNVPIY ...文字列:
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSSSL EK SYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQK EIT ALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F

UniProtKB: Actin, alpha skeletal muscle

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分子 #2: Tropomyosin alpha-1 chain

分子名称: Tropomyosin alpha-1 chain / タイプ: protein_or_peptide / ID: 2
詳細: Only the central section (residues 45-210) was modeled.
コピー数: 2 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 32.763621 KDa
組換発現生物種: Escherichia coli (大腸菌)
配列文字列: MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLN RRIQLVEEEL DRAQERLATA LQKLEEAEKA ADESERGMKV IESRAQKDEE KMEIQEIQLK EAKHIAEDAD R KYEEVARK ...文字列:
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLN RRIQLVEEEL DRAQERLATA LQKLEEAEKA ADESERGMKV IESRAQKDEE KMEIQEIQLK EAKHIAEDAD R KYEEVARK LVIIESDLER AEERAELSEG KCAELEEELK TVTNNLKSLE AQAEKYSQKE DRYEEEIKVL SDKLKEAETR AE FAERSVT KLEKSIDDLE DELYAQKLKY KAISEELDHA LNDMTSI

UniProtKB: Tropomyosin alpha-1 chain

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分子 #3: Myosin-7

分子名称: Myosin-7 / タイプ: protein_or_peptide / ID: 3
詳細: Residues 1-35, 200-216, 624-641, and 777-850 were disordered and not modeled.
コピー数: 3 / 光学異性体: LEVO
由来(天然)生物種: Bos taurus (ウシ) / 組織: Masseter Muscle
分子量理論値: 97.446898 KDa
配列文字列: MVDAEMAAFG EAAPYLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAT ILSREGGKVT AETEHGKTVT VKEDQVLQQN PPKFDKIED MAMLTFLHEP AVLYNLKERY ASWMIYTYSG LFCVTINPYK WLPVYNAEVV AAYRGKKRSE APPHIFSISD N AYQYMLTD ...文字列:
MVDAEMAAFG EAAPYLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAT ILSREGGKVT AETEHGKTVT VKEDQVLQQN PPKFDKIED MAMLTFLHEP AVLYNLKERY ASWMIYTYSG LFCVTINPYK WLPVYNAEVV AAYRGKKRSE APPHIFSISD N AYQYMLTD RENQSILITG ESGAGKTVNT KRVIQYFAVI AAIGDRSKKE QATGKGTLED QIIQANPALE AFGNAKTVRN DN SSRFGKF IRIHFGATGK LASADIETYL LEKSRVIFQL KAERDYHIFY QILSNKKPEL LDMLLITNNP YDYAFISQGE TTV ASIDDA EELMATDNAF DVLGFTTEEK NSMYKLTGAI MHFGNMKFKL KQREEQAEPD GTEEADKSAY LMGLNSADLL KGLC HPRVK VGNEYVTKGQ NVQQVVYAKG ALAKAVYERM FNWMVTRINA TLETKQPRQY FIGVLDIAGF EIFDFNSFEQ LCINF TNEK LQQFFNHHMF VLEQEEYKKE GIEWEFIDFG MDLQACIDLI EKPMGIMSIL EEECMFPKAT DMTFKAKLFD NHLGKS SNF QKPRNIKGKP EAHFSLIHYA GTVDYNIIGW LQKNKDPLNE TVVDLYKKSS LKMLSSLFAN YAGFDTPIEK GKGKAKK GS SFQTVSALHR ENLNKLMTNL RSTHPHFVRC IIPNETKSPG VIDNPLVMHQ LRCNGVLEGI RICRKGFPNR ILYGDFRQ R YRILNPAAIP EGQFIDSRKG AEKLLGSLDI DHNQYKFGHT KVFFKAGLLG LLEEMRDERL SRIITRIQAQ SRGVLSRME FKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL KSAETEKEIA

UniProtKB: Myosin-7

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分子 #4: ADENOSINE-5'-DIPHOSPHATE

分子名称: ADENOSINE-5'-DIPHOSPHATE / タイプ: ligand / ID: 4 / コピー数: 3 / 式: ADP
分子量理論値: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子*YM

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分子 #5: MAGNESIUM ION

分子名称: MAGNESIUM ION / タイプ: ligand / ID: 5 / コピー数: 3 / 式: MG
分子量理論値: 24.305 Da

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実験情報

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構造解析

手法クライオ電子顕微鏡法
解析らせん対称体再構成法
試料の集合状態helical array

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試料調製

濃度.525 mg/mL
緩衝液pH: 7
構成要素:
濃度式名称
50.0 mMCH3COONaSodium Acetate
3.0 mMMgCl2Magnesium Chloride
1.0 mMDithiothreitol
10.0 nMHEPES
グリッドモデル: Quantifoil R2/1 / 材質: COPPER / メッシュ: 200 / 支持フィルム - 材質: CARBON / 支持