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- PDB-1uk5: Solution structure of the Murine BAG domain of Bcl2-associated at... -

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Basic information

Entry
Database: PDB / ID: 1uk5
TitleSolution structure of the Murine BAG domain of Bcl2-associated athanogene 3
ComponentsBAG-family molecular chaperone regulator-3
KeywordsCHAPERONE / Triple Helix Bandle / CAIR-1 / Bis / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics
Function / homology
Function and homology information


striated muscle cell apoptotic process / Regulation of HSF1-mediated heat shock response / negative regulation of striated muscle cell apoptotic process / adenyl-nucleotide exchange factor activity / negative regulation of protein targeting to mitochondrion / positive regulation of aggrephagy / protein folding chaperone complex / muscle cell cellular homeostasis / spinal cord development / extrinsic apoptotic signaling pathway via death domain receptors ...striated muscle cell apoptotic process / Regulation of HSF1-mediated heat shock response / negative regulation of striated muscle cell apoptotic process / adenyl-nucleotide exchange factor activity / negative regulation of protein targeting to mitochondrion / positive regulation of aggrephagy / protein folding chaperone complex / muscle cell cellular homeostasis / spinal cord development / extrinsic apoptotic signaling pathway via death domain receptors / cellular response to unfolded protein / extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of protein export from nucleus / Z disc / positive regulation of protein import into nucleus / cellular response to mechanical stimulus / protein-folding chaperone binding / cellular response to heat / protein stabilization / ciliary basal body / protein-containing complex binding / mitochondrion / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
BAG domain / Molecular chaperone regulator BAG / BAG domain superfamily / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily ...BAG domain / Molecular chaperone regulator BAG / BAG domain superfamily / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
BAG family molecular chaperone regulator 3
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR
AuthorsHatta, R. / Yoshida, M. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: Structure / Year: 2010
Title: The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
Authors: Arakawa, A. / Handa, N. / Ohsawa, N. / Shida, M. / Kigawa, T. / Hayashi, F. / Shirouzu, M. / Yokoyama, S.
History
DepositionAug 19, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 19, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 650HELIX DETERMINATION METHOD: AUTHOR DETERMINED

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BAG-family molecular chaperone regulator-3


Theoretical massNumber of molelcules
Total (without water)11,8321
Polymers11,8321
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 / 100structures with the least restraint violations, target function
RepresentativeModel #1lowest energy

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Components

#1: Protein BAG-family molecular chaperone regulator-3 / Bcl2-associated athanogene 3 / BCL-2 binding athanogene-3 / BAG-3 / Bcl-2-binding protein Bis


Mass: 11832.287 Da / Num. of mol.: 1 / Fragment: BAG domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: FANTOM 2 cDNA 4931440G06 / Plasmid: P020122-09 / Production host: Cell-free synthesis (others) / References: UniProt: Q9JLV1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

DetailsContents: 0.7mM 13C, 15N-labeled protein, 20mM phosphate buffer, 90mM NaCl, 40mM MgSO4, 0.4mM NaN3, 8% D2O
Solvent system: 92% H2O, 8% D2O
Sample conditionsIonic strength: 250mM / pH: 6.5 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1CVARIANcollection
NMRPipe20020425DELAGLIO, F.processing
NMRView5.0.4Johnson, B.A.data analysis
KUJIRA0.823Kobayashi, N.data analysis
CYANA1.0.7Guentert, P.structure solution
CYANA1.0.7Guentert, P.refinement
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations, target function
Conformers calculated total number: 100 / Conformers submitted total number: 20

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