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- PDB-1tof: THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1tof
TitleTHIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES
ComponentsTHIOREDOXIN H
KeywordsELECTRON TRANSPORT / OXIDOREDUCTASE
Function / homology
Function and homology information


protein-disulfide reductase activity / cytosol
Similarity search - Function
Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesChlamydomonas reinhardtii (plant)
MethodSOLUTION NMR
AuthorsMittard, V. / Blackledge, M.J. / Stein, M. / Jacquot, J.-P. / Marion, D. / Lancelin, J.-M.
Citation
Journal: Eur.J.Biochem. / Year: 1997
Title: NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii.
Authors: Mittard, V. / Blackledge, M.J. / Stein, M. / Jacquot, J.P. / Marion, D. / Lancelin, J.M.
#1: Journal: Plant Mol.Biol. / Year: 1995
Title: Chlamydomonas Reinhardtii Thioredoxins: Structure of the Genes Coding for the Chloroplastic M and Cytosolic H Isoforms; Expression in Escherichia Coli of the Recombinant Proteins, Purification ...Title: Chlamydomonas Reinhardtii Thioredoxins: Structure of the Genes Coding for the Chloroplastic M and Cytosolic H Isoforms; Expression in Escherichia Coli of the Recombinant Proteins, Purification and Biochemical Properties
Authors: Stein, M. / Jacquot, J.P. / Jeannette, E. / Decottignies, P. / Hodges, M. / Lancelin, J.M. / Mittard, V. / Schmitter, J.M. / Miginiac-Maslow, M.
#2: Journal: Eur.J.Biochem. / Year: 1995
Title: 1H, 13C, 15N-NMR Resonance Assignments of Oxidized Thioredoxin H from the Eukaryotic Green Alga Chlamydomonas Reinhardtii Using New Methods Based on Two-Dimensional Triple-Resonance NMR ...Title: 1H, 13C, 15N-NMR Resonance Assignments of Oxidized Thioredoxin H from the Eukaryotic Green Alga Chlamydomonas Reinhardtii Using New Methods Based on Two-Dimensional Triple-Resonance NMR Spectroscopy and Computer-Assisted Backbone Assignment
Authors: Mittard, V. / Morelle, N. / Brutscher, B. / Simorre, J.P. / Marion, D. / Stein, M. / Jacquot, J.P. / Lirsac, P.N. / Lancelin, J.M.
History
DepositionMay 30, 1996Processing site: BNL
Revision 1.0Dec 7, 1996Provider: 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: 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_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: THIOREDOXIN H


Theoretical massNumber of molelcules
Total (without water)11,7281
Polymers11,7281
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)23 / -
Representative

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Components

#1: Protein THIOREDOXIN H / HTRX / HCH1 / CH1


Mass: 11727.534 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydomonas reinhardtii (plant) / Strain: CW15 / Cellular location: CYTOPLASM / Gene: THIOREDOXIN H CDNA (X78822 EMB / Plasmid: PET-3D / Species (production host): Escherichia coli / Gene (production host): THIOREDOXIN H CDNA (X78822,EMBL) / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P80028

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: Discover / Developer: BIOSYM / Classification: refinement
NMR ensembleConformers submitted total number: 23

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