[English] 日本語
Yorodumi- EMDB-0729: Structure of human cardiac thin filament in the calcium bound state -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0729 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of human cardiac thin filament in the calcium bound state | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | Troponin / Tropomyosin / Actin / Thin filement / Muscle / CONTRACTILE PROTEIN-ACTIN BINDING PROTEIN complex | |||||||||
Function / homology | Function and homology information positive regulation of heart rate by epinephrine / muscle thin filament tropomyosin / regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / cardiac Troponin complex / cardiac myofibril ...positive regulation of heart rate by epinephrine / muscle thin filament tropomyosin / regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / cardiac Troponin complex / cardiac myofibril / regulation of smooth muscle contraction / troponin complex / bleb / negative regulation of vascular associated smooth muscle cell migration / regulation of muscle contraction / muscle filament sliding / transition between fast and slow fiber / negative regulation of ATP-dependent activity / ruffle organization / Striated Muscle Contraction / positive regulation of ATP-dependent activity / regulation of cardiac muscle contraction by calcium ion signaling / response to metal ion / regulation of heart contraction / structural constituent of muscle / sarcomere organization / cytoskeletal motor activator activity / ventricular cardiac muscle tissue morphogenesis / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / heart contraction / troponin I binding / actin filament bundle / filamentous actin / negative regulation of vascular associated smooth muscle cell proliferation / actin filament bundle assembly / skeletal muscle thin filament assembly / striated muscle thin filament / skeletal muscle myofibril / skeletal muscle contraction / actin monomer binding / positive regulation of cell adhesion / Smooth Muscle Contraction / calcium channel inhibitor activity / vasculogenesis / skeletal muscle fiber development / stress fiber / cytoskeleton organization / titin binding / cardiac muscle contraction / Ion homeostasis / positive regulation of stress fiber assembly / actin filament polymerization / cytoskeletal protein binding / sarcomere / negative regulation of cell migration / filopodium / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / wound healing / structural constituent of cytoskeleton / intracellular calcium ion homeostasis / ruffle membrane / cellular response to reactive oxygen species / response to calcium ion / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / lamellipodium / cell body / actin binding / heart development / regulation of cell shape / cytoskeleton / hydrolase activity / protein heterodimerization activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / protein kinase binding / magnesium ion binding / protein homodimerization activity / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) / Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.8 Å | |||||||||
Authors | Fujii T / Yamada Y | |||||||||
Citation | Journal: Nat Commun / Year: 2020 Title: Cardiac muscle thin filament structures reveal calcium regulatory mechanism. Authors: Yurika Yamada / Keiichi Namba / Takashi Fujii / Abstract: Contraction of striated muscles is driven by cyclic interactions of myosin head projecting from the thick filament with actin filament and is regulated by Ca released from sarcoplasmic reticulum. ...Contraction of striated muscles is driven by cyclic interactions of myosin head projecting from the thick filament with actin filament and is regulated by Ca released from sarcoplasmic reticulum. Muscle thin filament consists of actin, tropomyosin and troponin, and Ca binding to troponin triggers conformational changes of troponin and tropomyosin to allow actin-myosin interactions. However, the structural changes involved in this regulatory mechanism remain unknown. Here we report the structures of human cardiac muscle thin filament in the absence and presence of Ca by electron cryomicroscopy. Molecular models in the two states built based on available crystal structures reveal the structures of a C-terminal region of troponin I and an N-terminal region of troponin T in complex with the head-to-tail junction of tropomyosin together with the troponin core on actin filament. Structural changes of the thin filament upon Ca binding now reveal the mechanism of Ca regulation of muscle contraction. | |||||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_0729.map.gz | 23.3 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-0729-v30.xml emd-0729.xml | 16.1 KB 16.1 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_0729_fsc.xml | 7.1 KB | Display | FSC data file |
Images | emd_0729.png | 45.6 KB | ||
Filedesc metadata | emd-0729.cif.gz | 5.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0729 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0729 | HTTPS FTP |
-Related structure data
Related structure data | 6kn8MC 7utiM 0728C 6kn7C M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_0729.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 2.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Sample components
+Entire : Cardiac muscle thin filament in the calcium bound state
+Supramolecule #1: Cardiac muscle thin filament in the calcium bound state
+Supramolecule #2: Actin, alpha skeletal muscle
+Supramolecule #3: Tropomyosin, Troponin
+Macromolecule #1: Actin, alpha skeletal muscle
+Macromolecule #2: Tropomyosin alpha-1 chain
+Macromolecule #3: Tropomyosin alpha-1 chain
+Macromolecule #4: Troponin T, cardiac muscle
+Macromolecule #5: Troponin I, cardiac muscle
+Macromolecule #6: Troponin C, slow skeletal and cardiac muscles
+Macromolecule #7: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Concentration | 0.05 mg/mL |
---|---|
Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | JEOL CRYO ARM 200 |
---|---|
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 65.0 e/Å2 |