|Entry||Database: EMDB / ID: EMD-7330|
|Title||High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing|
|Sample||Complex of actin, myosin-1b, and calmodulin with ADP:|
Unconventional myosin-Ib / Calmodulin / Actin, alpha skeletal muscle / (ligand) x 2
|Function / homology|
Function and homology information
actin filament-based movement / transferrin transport / vesicle transport along actin filament / CaM pathway / Sodium/Calcium exchangers / Cam-PDE 1 activation / Reduction of cytosolic Ca++ levels / microfilament motor activity / Calmodulin induced events / => GO:0120081 ...actin filament-based movement / transferrin transport / vesicle transport along actin filament / CaM pathway / Sodium/Calcium exchangers / Cam-PDE 1 activation / Reduction of cytosolic Ca++ levels / microfilament motor activity / Calmodulin induced events / => GO:0120081 / microfilament motor activity => GO:0000146 / Glycogen breakdown (glycogenolysis) / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / myosin complex / CLEC7A (Dectin-1) induces NFAT activation / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / glycogen catabolic process / PKA activation / CREB1 phosphorylation through the activation of Adenylate Cyclase / mesenchyme migration / establishment of protein localization to mitochondrial membrane / organelle localization by membrane tethering / CaMK IV-mediated phosphorylation of CREB / regulation of cardiac muscle cell action potential / negative regulation of high voltage-gated calcium channel activity / N-terminal myristoylation domain binding / autophagosome membrane docking / tropomyosin binding / mitochondrion-endoplasmic reticulum membrane tethering / myosin heavy chain binding / Phase 0 - rapid depolarisation / Activation of RAC1 downstream of NMDARs / troponin I binding / type 3 metabotropic glutamate receptor binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Ion transport by P-type ATPases / regulation of synaptic vesicle endocytosis / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of peptidyl-threonine phosphorylation / Unblocking of NMDA receptors, glutamate binding and activation / protein phosphatase activator activity / brush border / Synthesis of IP3 and IP4 in the cytosol / positive regulation of ryanodine-sensitive calcium-release channel activity / skeletal muscle thin filament assembly / actin filament bundle / striated muscle thin filament / filamentous actin / regulation of rhodopsin mediated signaling pathway / Smooth Muscle Contraction / response to corticosterone / catalytic complex / RHO GTPases activate PAKs / positive regulation of cyclic-nucleotide phosphodiesterase activity / Activation of AMPK downstream of NMDARs / adenylate cyclase binding / Long-term potentiation / inositol phosphate metabolic process / detection of calcium ion / phosphatidylinositol-3,4,5-trisphosphate binding / actin filament bundle assembly / actin monomer binding / Uptake and function of anthrax toxins / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / Protein methylation / cytoskeletal motor activity / skeletal muscle fiber development / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction / DARPP-32 events / skeletal muscle myofibril / adenylate cyclase activator activity / RHO GTPases activate IQGAPs / post-Golgi vesicle-mediated transport / calcium channel inhibitor activity / nitric-oxide synthase binding / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / positive regulation of phosphoprotein phosphatase activity / activation of adenylate cyclase activity / Inactivation, recovery and regulation of the phototransduction cascade / Ion homeostasis / stress fiber / trans-Golgi network membrane / voltage-gated potassium channel complex / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of heart rate / Wnt signaling pathway, calcium modulating pathway / titin binding / tetrahydrobiopterin metabolic process / substantia nigra development / eNOS activation / sarcomere / actin filament polymerization / positive regulation of protein dephosphorylation / calcium channel complex / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / phosphatidylinositol 3-kinase binding / regulation of ryanodine-sensitive calcium-release channel activity
Similarity search - Function
Class I myosin tail homology (TH1) domain profile. / Unconventional myosin tail, actin- and lipid-binding / Class I myosin tail homology domain / Class I myosin, motor domain / IQ calmodulin-binding motif / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin. Large ATPases. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. ...Class I myosin tail homology (TH1) domain profile. / Unconventional myosin tail, actin- and lipid-binding / Class I myosin tail homology domain / Class I myosin, motor domain / IQ calmodulin-binding motif / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin. Large ATPases. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / IQ motif profile. / IQ motif, EF-hand binding site / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actins and actin-related proteins signature. / Actin/actin-like conserved site / Actin / Actin / Actin family / Kinesin motor domain superfamily / EF-hand domain pair / ATPase, nucleotide binding domain / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand calcium-binding domain. / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Calmodulin-1 / Actin, alpha skeletal muscle / Unconventional myosin-Ib
Similarity search - Component
|Biological species||unidentified (others) / Rat (rat) / Rabbit (rabbit)|
|Method||helical reconstruction / cryo EM / Resolution: 3.8 Å|
|Authors||Mentes A / Huehn A / Liu X / Zwolak A / Dominguez R / Shuman H / Ostap EM / Sindelar CV|
|Funding support|| United States, 1 items |
|Citation||Journal: Proc Natl Acad Sci U S A / Year: 2018|
Title: High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing.
Authors: Ahmet Mentes / Andrew Huehn / Xueqi Liu / Adam Zwolak / Roberto Dominguez / Henry Shuman / E Michael Ostap / Charles V Sindelar /
Abstract: Myosins adjust their power outputs in response to mechanical loads in an isoform-dependent manner, resulting in their ability to dynamically adapt to a range of motile challenges. Here, we reveal the ...Myosins adjust their power outputs in response to mechanical loads in an isoform-dependent manner, resulting in their ability to dynamically adapt to a range of motile challenges. Here, we reveal the structural basis for force-sensing based on near-atomic resolution structures of one rigor and two ADP-bound states of myosin-IB (myo1b) bound to actin, determined by cryo-electron microscopy. The two ADP-bound states are separated by a 25° rotation of the lever. The lever of the first ADP state is rotated toward the pointed end of the actin filament and forms a previously unidentified interface with the N-terminal subdomain, which constitutes the upper half of the nucleotide-binding cleft. This pointed-end orientation of the lever blocks ADP release by preventing the N-terminal subdomain from the pivoting required to open the nucleotide binding site, thus revealing how myo1b is inhibited by mechanical loads that restrain lever rotation. The lever of the second ADP state adopts a rigor-like orientation, stabilized by class-specific elements of myo1b. We identify a role for this conformation as an intermediate in the ADP release pathway. Moreover, comparison of our structures with other myosins reveals structural diversity in the actomyosin binding site, and we reveal the high-resolution structure of actin-bound phalloidin, a potent stabilizer of filamentous actin. These results provide a framework to understand the spectrum of force-sensing capacities among the myosin superfamily.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_7330.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.3 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Projections & Slices|
-Half map: Actin-bound Myosin, half mask 1
|Annotation||Actin-bound Myosin, half mask 1|
|Projections & Slices|
-Half map: Actin-bound Myosin, half mask 2
+Entire Complex of actin, myosin-1b, and calmodulin with ADP
|Entire||Name: Complex of actin, myosin-1b, and calmodulin with ADP / Number of Components: 6|
+Component #1: protein, Complex of actin, myosin-1b, and calmodulin with ADP
|Protein||Name: Complex of actin, myosin-1b, and calmodulin with ADP / Recombinant expression: No|
|Source||Species: unidentified (others)|
+Component #2: protein, Unconventional myosin-Ib
|Protein||Name: Unconventional myosin-Ib / Number of Copies: 1 / Recombinant expression: No|
|Mass||Theoretical: 84.14393 kDa|
|Source||Species: Rat (rat)|
+Component #3: protein, Calmodulin
|Protein||Name: Calmodulin / Number of Copies: 1 / Recombinant expression: No|
|Mass||Theoretical: 16.72135 kDa|
|Source||Species: unidentified (others)|
+Component #4: protein, Actin, alpha skeletal muscle
|Protein||Name: Actin, alpha skeletal muscle / Number of Copies: 5 / Recombinant expression: No|
|Mass||Theoretical: 41.862613 kDa|
|Source||Species: Rabbit (rabbit)|
+Component #5: ligand, MAGNESIUM ION
|Ligand||Name: MAGNESIUM ION / Number of Copies: 6 / Recombinant expression: No|
|Mass||Theoretical: 2.430505 MDa|
+Component #6: ligand, ADENOSINE-5'-DIPHOSPHATE
|Ligand||Name: ADENOSINE-5'-DIPHOSPHATE / Number of Copies: 6 / Recombinant expression: No|
|Mass||Theoretical: 0.427201 kDa|
|Specimen||Specimen State: helical array / Method: cryo EM|
|Helical Parameters||Axial Symmetry: C1 (asymmetric) / Delta Z: 27.5 Å / Delta Phi: -167.4 %deg;|
|Sample solution||pH: 7|
|Vitrification||Cryogen Name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron Source: FIELD EMISSION GUN / Accelerating Voltage: 300 kV / Electron Dose: 50 e/Å2 / Illumination Mode: SPOT SCAN|
|Lens||Imaging Mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: helical reconstruction|
|3D reconstruction||Resolution: 3.8 Å / Resolution Method: FSC 0.143 CUT-OFF|
Details: Resolution estimated by post-processing in RELION using a mask with soft edges that included only the central subunit.
-Atomic model buiding
|Modeling #1||Refinement protocol: flexible / Refinement space: REAL|
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