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- PDB-1xbl: NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA ... -

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Basic information

Entry
Database: PDB / ID: 1xbl
TitleNMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES
ComponentsDNAJChaperone DnaJ
KeywordsCHAPERONE / DNA REPLICATION / HEAT SHOCK
Function / homology
Function and homology information


sigma factor antagonist activity / protein disulfide isomerase activity / chaperone cofactor-dependent protein refolding / protein unfolding / protein-disulfide reductase activity / heat shock protein binding / viral process / unfolded protein binding / protein folding / response to heat ...sigma factor antagonist activity / protein disulfide isomerase activity / chaperone cofactor-dependent protein refolding / protein unfolding / protein-disulfide reductase activity / heat shock protein binding / viral process / unfolded protein binding / protein folding / response to heat / protein-folding chaperone binding / protein refolding / protein-containing complex assembly / DNA replication / protein homodimerization activity / protein-containing complex / zinc ion binding / ATP binding / membrane / cytosol / cytoplasm
Similarity search - Function
Chaperone DnaJ / DnaJ central domain / Heat shock protein DnaJ, cysteine-rich domain / Zinc finger CR-type profile. / Heat shock protein DnaJ, cysteine-rich domain superfamily / DnaJ domain / HSP40/DnaJ peptide-binding / Chaperone DnaJ, C-terminal / DnaJ C terminal domain / Nt-dnaJ domain signature. ...Chaperone DnaJ / DnaJ central domain / Heat shock protein DnaJ, cysteine-rich domain / Zinc finger CR-type profile. / Heat shock protein DnaJ, cysteine-rich domain superfamily / DnaJ domain / HSP40/DnaJ peptide-binding / Chaperone DnaJ, C-terminal / DnaJ C terminal domain / Nt-dnaJ domain signature. / DnaJ domain, conserved site / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chaperone protein DnaJ
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / REDAC
AuthorsPellecchia, M. / Szyperski, T. / Wall, D. / Georgopoulos, C. / Wuthrich, K.
Citation
Journal: J.Mol.Biol. / Year: 1996
Title: NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
Authors: Pellecchia, M. / Szyperski, T. / Wall, D. / Georgopoulos, C. / Wuthrich, K.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994
Title: NMR Structure Determination of the Escherichia Coli Dnaj Molecular Chaperone: Secondary Structure and Backbone Fold of the N-Terminal Region (Residues 2-108) Containing the Highly Conserved J Domain
Authors: Szyperski, T. / Pellecchia, M. / Wall, D. / Georgopoulos, C. / Wuthrich, K.
History
DepositionOct 7, 1996Processing site: BNL
Revision 1.0Jan 11, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: DNAJ


Theoretical massNumber of molelcules
Total (without water)11,8461
Polymers11,8461
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 / 50TARGET FUNCTION (SEE PAPER *JRNL*)
Representative

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Components

#1: Protein DNAJ / Chaperone DnaJ


Mass: 11846.043 Da / Num. of mol.: 1
Fragment: N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P08622

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: SEE PAPER *JRNL*

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Sample preparation

Sample conditionspH: 6.0 / Temperature: 301 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
OPALLUGINBHUL,GUNTERT,BILLETERrefinement
DIANAstructure solution
RefinementMethod: REDAC / Software ordinal: 1
NMR ensembleConformer selection criteria: TARGET FUNCTION (SEE PAPER *JRNL*)
Conformers calculated total number: 50 / Conformers submitted total number: 20

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