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- PDB-2n13: Complex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb -

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Basic information

Entry
Database: PDB / ID: 2n13
TitleComplex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb
Components
  • (Ubiquitin) x 2
  • Unconventional myosin-VI
KeywordsMOTOR PROTEIN/PROTEIN BINDING / MOTOR PROTEIN-PROTEIN BINDING complex
Function / homology
Function and homology information


regulation of secretion / minus-end directed microfilament motor activity / unconventional myosin complex / inner ear auditory receptor cell differentiation / actin filament-based movement / clathrin-coated vesicle membrane / Gap junction degradation / Trafficking of AMPA receptors / symbiont entry into host cell via disruption of host cell glycocalyx / RHOBTB1 GTPase cycle ...regulation of secretion / minus-end directed microfilament motor activity / unconventional myosin complex / inner ear auditory receptor cell differentiation / actin filament-based movement / clathrin-coated vesicle membrane / Gap junction degradation / Trafficking of AMPA receptors / symbiont entry into host cell via disruption of host cell glycocalyx / RHOBTB1 GTPase cycle / inner ear morphogenesis / symbiont entry into host cell via disruption of host cell envelope / microfilament motor activity / virus tail / filamentous actin / microvillus / cytoskeletal motor activity / RHOU GTPase cycle / endocytic vesicle / RHOBTB2 GTPase cycle / ruffle / clathrin-coated pit / autophagosome / actin filament organization / actin filament / filopodium / DNA damage response, signal transduction by p53 class mediator / intracellular protein transport / sensory perception of sound / ADP binding / ruffle membrane / endocytosis / actin filament binding / apical part of cell / intracellular protein localization / actin cytoskeleton / actin binding / cytoplasmic vesicle / cell cortex / nuclear membrane / calmodulin binding / endosome / response to xenobiotic stimulus / lysosomal membrane / perinuclear region of cytoplasm / Golgi apparatus / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Myosin VI, cargo binding domain / Class VI myosin, motor domain / : / Myosin VI cargo binding domain / Myosin VI, lever arm / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Pectate lyase superfamily protein / Rhamnogalacturonase A/epimerase, pectate lyase-like ...Myosin VI, cargo binding domain / Class VI myosin, motor domain / : / Myosin VI cargo binding domain / Myosin VI, lever arm / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Pectate lyase superfamily protein / Rhamnogalacturonase A/epimerase, pectate lyase-like / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / Pectin lyase fold / Pectin lyase fold/virulence factor / Kinesin motor domain superfamily / Ubiquitin family / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Tail fiber / Unconventional myosin-VI
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model1
AuthorsHe, F. / Walters, K.
CitationJournal: Cell Rep / Year: 2016
Title: Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains.
Authors: He, F. / Wollscheid, H.P. / Nowicka, U. / Biancospino, M. / Valentini, E. / Ehlinger, A. / Acconcia, F. / Magistrati, E. / Polo, S. / Walters, K.J.
History
DepositionMar 20, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Mar 9, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 30, 2016Group: Database references
Revision 1.2Apr 6, 2016Group: Database references
Revision 1.3Jun 14, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.4Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Unconventional myosin-VI
B: Ubiquitin
C: Ubiquitin
D: Unconventional myosin-VI


Theoretical massNumber of molelcules
Total (without water)27,6544
Polymers27,6544
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Unconventional myosin-VI / Unconventional myosin-6


Mass: 5212.982 Da / Num. of mol.: 2 / Fragment: K63R, G76C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KIAA0389, MYO6 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UM54
#2: Protein Ubiquitin / Ubiquitin


Mass: 8604.845 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG47
#3: Protein Ubiquitin


Mass: 8622.922 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG47
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-15N NOESY
1213D 1H-13C NOESY
1313D half-filter NOESY

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Sample preparation

DetailsContents: 0.5 mM [U-13C; U-15N] protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O
SampleConc.: 0.5 mM / Component: entity-1 / Isotopic labeling: [U-13C; U-15N]
Sample conditionsIonic strength: 50 / pH: 6.5 / Pressure: ambient / Temperature: 283 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz

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Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
KUJIRANaohiro Kobayashichemical shift assignment
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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