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Basic information

Entry
Database: PDB / ID: 2ju5
TitleDsbH Oxidoreductase
ComponentsThioredoxin Disulfide Isomerase
KeywordsOXIDOREDUCTASE / protein
Function / homology
Function and homology information


Oxidoreductases; Acting on a sulfur group of donors / periplasmic space / oxidoreductase activity
Similarity search - Function
Thioredoxin-like / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Disulfide bond reductase DsbH
Similarity search - Component
Biological speciesChlamydophila pneumoniae (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsUlmer, T.S.
CitationJournal: J.Biol.Chem. / Year: 2008
Title: Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase.
Authors: Mac, T.T. / von Hacht, A. / Hung, K.C. / Dutton, R.J. / Boyd, D. / Bardwell, J.C. / Ulmer, T.S.
History
DepositionAug 15, 2007Deposition site: BMRB / Processing site: RCSB
Revision 1.0Nov 27, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.2Feb 19, 2020Group: Data collection / Database references / Other
Category: pdbx_database_status / pdbx_nmr_software ...pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name ..._pdbx_database_status.status_code_cs / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.3Oct 20, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Jun 14, 2023Group: Other / Category: pdbx_database_status / Item: _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Thioredoxin Disulfide Isomerase


Theoretical massNumber of molelcules
Total (without water)17,6711
Polymers17,6711
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 / 20all calculated structures submitted
RepresentativeModel #1lowest energy

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Components

#1: Protein Thioredoxin Disulfide Isomerase


Mass: 17671.027 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydophila pneumoniae (bacteria) / Strain: TW-183 / Plasmid: pET44-DsbH / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Z6Y0

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-13C NOESY
1213D 1H-15N NOESY
1313D HNCO
1413D HN(CA)CB
1513D HNCA
1613D CBCA(CO)NH

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Sample preparation

DetailsContents: 1.0 mM [U-99% 13C; U-99% 15N] DsbH, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
SampleConc.: 1.0 mM / Component: DsbH / Isotopic labeling: [U-99% 13C; U-99% 15N]
Sample conditionsIonic strength: 100 mM / pH: 6.0 / Pressure: ambient / Temperature: 298.2 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR softwareName: X-PLOR NIH / Developer: Schwieters, C.D. et al. / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 20 / Conformers submitted total number: 20

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