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- PDB-2btt: NMR Structure of MYO3-SH3 domain from Myosin-typeI from S. cerevisiae -

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Basic information

Entry
Database: PDB / ID: 2btt
TitleNMR Structure of MYO3-SH3 domain from Myosin-typeI from S. cerevisiae
ComponentsMYOSIN-3 ISOFORM
KeywordsCONTRACTILE PROTEIN / SH3 DOMAIN / MYOSIN-TYPE I / MUSCLE PROTEIN / ACTIN-BINDING / ATP-BINDING / MOTOR PROTEIN / MYOSIN / NUCLEOTIDE-BINDING / PHOSPHORYLATION
Function / homology
Function and homology information


bipolar cellular bud site selection / myosin I complex / actin cortical patch localization / positive regulation of Arp2/3 complex-mediated actin nucleation / cell tip / fungal-type cell wall organization / actin cortical patch / vesicle transport along actin filament / response to osmotic stress / microfilament motor activity ...bipolar cellular bud site selection / myosin I complex / actin cortical patch localization / positive regulation of Arp2/3 complex-mediated actin nucleation / cell tip / fungal-type cell wall organization / actin cortical patch / vesicle transport along actin filament / response to osmotic stress / microfilament motor activity / myosin binding / exocytosis / actin filament organization / cell periphery / endocytosis / actin filament binding / actin cytoskeleton / vesicle / hydrolase activity / ATP binding / plasma membrane / cytoplasm
Similarity search - Function
Fungal myosin-I, SH3 domain / Class I myosin tail homology domain / Class I myosin, motor domain / Unconventional myosin tail, actin- and lipid-binding / Class I myosin tail homology (TH1) domain profile. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / SH3 Domains ...Fungal myosin-I, SH3 domain / Class I myosin tail homology domain / Class I myosin, motor domain / Unconventional myosin tail, actin- and lipid-binding / Class I myosin tail homology (TH1) domain profile. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / SH3 Domains / Kinesin motor domain superfamily / SH3 domain / SH3 type barrels. / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodSOLUTION NMR / ARIA 1.2
AuthorsMusi, V. / Birdsall, B. / Pastore, A.
CitationJournal: Protein Sci. / Year: 2006
Title: New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.
Authors: Musi, V. / Birdsall, B. / Fernandez-Ballester, G. / Guerrini, R. / Salvatori, S. / Serrano, L. / Pastore, A.
History
DepositionJun 6, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 12, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Database references / Category: citation
Item: _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title
Revision 1.4Jan 15, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name
Revision 1.5Apr 24, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MYOSIN-3 ISOFORM


Theoretical massNumber of molelcules
Total (without water)7,5881
Polymers7,5881
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein MYOSIN-3 ISOFORM / MYO3-SH3 DOMAIN / MYO3-SH3 ISOFORM


Mass: 7588.495 Da / Num. of mol.: 1 / Fragment: SH3 DOMAIN, RESIDUES 1122-1190
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P36006

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1111H-15N-NOESY-HSQC
1211H-15N- TOCSY-HSQC
131HNHA
141HNHB
151CBCA(CO)NH
161CBCANH
171HNCO
181(H)CCH- TOCSY
1912D-NOESY
11012D COSY
11112D-TOCSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED MYO3_SH3.

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Sample preparation

DetailsContents: 90% WATER/10% D2O
Sample conditionsIonic strength: 50 mM / pH: 7.0 / Pressure: 1.0 atm / Temperature: 298.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA6002
Varian INOVAVarianINOVA8003

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Processing

NMR software
NameVersionDeveloperClassification
ARIA1.2LINGE,HABECK,RIEPING,NILGESrefinement
XEASYstructure solution
Sparkystructure solution
RefinementMethod: ARIA 1.2 / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 20

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