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- PDB-7rb9: Cryo-EM structure of the rigor state Jordan myosin-15-F-actin complex -
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Open data
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Basic information
Entry | Database: PDB / ID: 7rb9 | ||||||||||||
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Title | Cryo-EM structure of the rigor state Jordan myosin-15-F-actin complex | ||||||||||||
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![]() | MOTOR PROTEIN/ATP Binding Protein / myosin motor proteins / actin cytoskeleton / stereocilia / deafness / MOTOR PROTEIN / MOTOR PROTEIN-ATP Binding Protein complex | ||||||||||||
Function / homology | ![]() actin-based cell projection / stereocilium bundle / Striated Muscle Contraction / stereocilium / myosin complex / inner ear morphogenesis / microfilament motor activity / skeletal muscle thin filament assembly / striated muscle thin filament / response to light stimulus ...actin-based cell projection / stereocilium bundle / Striated Muscle Contraction / stereocilium / myosin complex / inner ear morphogenesis / microfilament motor activity / skeletal muscle thin filament assembly / striated muscle thin filament / response to light stimulus / skeletal muscle fiber development / stress fiber / actin filament organization / locomotory behavior / actin filament / sensory perception of sound / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / endocytosis / actin filament binding / actin cytoskeleton / hydrolase activity / ATP binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.76 Å | ||||||||||||
![]() | Gong, R. / Reynolds, M.J. / Gurel, P. / Alushin, G.M. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia. Authors: Rui Gong / Fangfang Jiang / Zane G Moreland / Matthew J Reynolds / Santiago Espinosa de Los Reyes / Pinar Gurel / Arik Shams / James B Heidings / Michael R Bowl / Jonathan E Bird / Gregory M Alushin / ![]() ![]() Abstract: The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin ...The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, ""). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height. #1: ![]() Title: Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia Authors: Gong, R. / Jiang, F. / Moreland, Z.G. / Reynolds, M.J. / Gurel, P.S. / Shams, A. / Bowl, M.R. / Bird, J.E. / Alushin, G.M. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 318.7 KB | Display | ![]() |
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PDB format | ![]() | 259.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 24400MC ![]() 7r8vC ![]() 7r91C ![]() 7rb8C ![]() 7udtC ![]() 7uduC C: citing same article ( M: map data used to model this data |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 41631.430 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | | Mass: 78124.672 Da / Num. of mol.: 1 / Mutation: D1647G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() References: UniProt: Q9QZZ4 #3: Chemical | #4: Chemical | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
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Molecular weight | Value: 5.4 kDa/nm / Experimental value: YES | ||||||||||||||||||||||||
Source (natural) |
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Buffer solution | pH: 7 Details: 10 mM imidazole pH 7.0, 50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 0.5 mM DTT, 0.01% NaN3 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: C-flat-1.2/1.3 | ||||||||||||||||||||||||
Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 293 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 29000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 1500 nm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 10 sec. / Electron dose: 60 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 |
Image scans | Movie frames/image: 40 / Used frames/image: 1-40 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -166.66 ° / Axial rise/subunit: 27.08 Å / Axial symmetry: C1 | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 113662 | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.76 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 91340 / Symmetry type: HELICAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 6BNO |