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- PDB-2gt3: Solution structure and dynamics of the reduced form of Methionine... -

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Basic information

Entry
Database: PDB / ID: 2gt3
TitleSolution structure and dynamics of the reduced form of Methionine Sulfoxide Reductase A from Escherichia coli, a 23 kDa protein
ComponentsMethionine Sulfoxide Reductase A
KeywordsOXIDOREDUCTASE / L-methionine sulfoxide / Met-(S)-SO / L-methionine-(S)-sulfoxide / Met-(R)-SO / L-methionine-(R)-sulfoxide / Msr / methionine sulfoxide reductase / nuclear magnetic resonance / HSQC / heteronuclear single quantum coherence / NOE / nuclear Overhauser effect / NOESY / NOE spectroscopy / RDC / residual dipolar coupling / rms / root mean square / rmsd / rms deviation / ROS / reactive oxygen species.
Function / homology
Function and homology information


L-methionine-(S)-S-oxide reductase activity / oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor / peptide-methionine (S)-S-oxide reductase / peptide-methionine (S)-S-oxide reductase activity / protein repair / protein modification process / cellular response to oxidative stress / response to oxidative stress / cytosol / cytoplasm
Similarity search - Function
Peptide Methionine Sulfoxide Reductase; Chain A / Peptide methionine sulphoxide reductase MsrA / Peptide methionine sulphoxide reductase MsrA domain / Peptide methionine sulphoxide reductase MsrA superfamily / Peptide methionine sulfoxide reductase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Peptide methionine sulfoxide reductase MsrA
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsCoudevylle, N. / Cung, M.T.
CitationJournal: J.Mol.Biol. / Year: 2007
Title: Solution Structure and Backbone Dynamics of the Reduced Form and an Oxidized Form of E. coli Methionine Sulfoxide Reductase A (MsrA): Structural Insight of the MsrA Catalytic Cycle.
Authors: Coudevylle, N. / Antoine, M. / Bouguet-Bonnet, S. / Mutzenhardt, P. / Boschi-Muller, S. / Branlant, G. / Cung, M.T.
History
DepositionApr 27, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 27, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_spectrometer ...database_2 / pdbx_nmr_spectrometer / 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_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Methionine Sulfoxide Reductase A


Theoretical massNumber of molelcules
Total (without water)23,3361
Polymers23,3361
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 / 1000target function
RepresentativeModel #1fewest violations

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Components

#1: Protein Methionine Sulfoxide Reductase A / reductase


Mass: 23335.982 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A744, EC: 1.8.4.6

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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: 1 mM MsrA, 1mM DTT, 50 mM KPi, pH 7.1, 90 % H2O, 10 % D2O
Solvent system: 90% H2O/10% D2O
Sample conditionspH: 7.1 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionClassification
DYANA2structure solution
DYANA2refinement
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 1000 / Conformers submitted total number: 20

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