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- PDB-2n9b: Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coil... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n9b | ||||||
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Title | Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil | ||||||
![]() | Unconventional myosin-X, General control protein GCN4 fusion | ||||||
![]() | MOTOR PROTEIN/TRANSCRIPTION / anti-parallel coiled-coil / coiled-coil / MOTOR PROTEIN-TRANSCRIPTION complex | ||||||
Function / homology | ![]() plus-end directed microfilament motor activity / filopodium tip / protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / regulation of filopodium assembly / cytoskeleton-dependent intracellular transport / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II ...plus-end directed microfilament motor activity / filopodium tip / protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / regulation of filopodium assembly / cytoskeleton-dependent intracellular transport / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / filopodium membrane / myosin complex / microfilament motor activity / phosphatidylinositol-3,4,5-trisphosphate binding / TFIID-class transcription factor complex binding / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / amino acid biosynthetic process / ruffle / cellular response to amino acid starvation / filopodium / RNA polymerase II transcription regulator complex / : / actin filament binding / lamellipodium / cell cortex / regulation of cell shape / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / sequence-specific DNA binding / calmodulin binding / DNA-binding transcription factor activity, RNA polymerase II-specific / regulation of cell cycle / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Vavra, K.C. / Xia, Y. / Rock, R.S. | ||||||
![]() | ![]() Title: Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection Authors: Vavra, K.C. / Xia, Y. / Rock, R.S. #1: ![]() Title: Antiparallel coiled-coil-mediated dimerization of myosin X. Authors: Lu, Q. / Ye, F. / Wei, Z. / Wen, Z. / Zhang, M. #2: ![]() Title: X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil Authors: Klemm, J.D. / Kim, P.S. / Alber, T. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 2008 Title: A myosin motor that selects bundled actin for motility Authors: Nagy, S. / Ricca, B.L. / Norstrom, M.F. / Courson, D.F. / Brawley, C.M. / Smithback, P.A. / Rock, R.S. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Spare the rod, spoil the regulation: necessity for a myosin rod Authors: Trybus, K.M. / Freyzon, Y. / Faust, L.Z. / Sweeney, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 456.2 KB | Display | ![]() |
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PDB format | ![]() | 386.1 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 537.9 KB | Display | ![]() |
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Full document | ![]() | 738.7 KB | Display | |
Data in XML | ![]() | 35.7 KB | Display | |
Data in CIF | ![]() | 48.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 8200.290 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Gene: MYO10, GCN4, AAS3, ARG9, YEL009C / Strain: ATCC 204508 / S288c / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Tandem antiparallel coiled-coil fusion derived from Bos taurus myosin-10 coiled-coil and GCN4-p1. Structure solved by solution NMR. Tertiary structure supported by Small-Angle X-ray scattering (see reference). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.1 mM [U-100% 13C; U-100% 15N] entity-1, 100 mM potassium phosphate-2, 1 mM EDTA-3, 0.03 % sodium azide-4, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.6 / pH: 6.5 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1561 / NOE intraresidue total count: 332 / NOE long range total count: 149 / NOE medium range total count: 610 / NOE sequential total count: 470 / Hydrogen bond constraints total count: 294 / Protein phi angle constraints total count: 147 / Protein psi angle constraints total count: 147 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |