Structural Insights into Interaction between Mammalian Methionine Sulfoxide Reductase B1 and Thioredoxin

Maintenance of the cellular redox balance has vital importance for correcting organism functioning. Methionine sulfoxide reductases (Msrs) are among the key members of the cellular antioxidant defence system. To work properly, methionine sulfoxide reductases need to be reduced by their biological partner, thioredoxin (Trx). This process, according to the available kinetic data, represents the slowest step in the Msrs catalytic cycle. In the present paper, we investigated structural aspects of the intermolecular complex formation between mammalian MsrB1 and Trx. NMR spectroscopy and biocomputing were the two mostly used through the research approaches. The formation of NMR detectable MsrB1/Trx complex was monitored and studied in attempt to understand MsrB1 reduction mechanism. Using NMR data, molecular mechanics, protein docking, and molecular dynamics simulations, it was found that intermediate MsrB1/Trx complex is stabilized by interprotein β-layer. The complex formation accompanied by distortion of disulfide bond within MsrB1 facilitates the reduction of oxidized MsrB1 as it is evidenced by the obtained data.

• Publication year

  2012

• Venue

  Journal of Biomedicine and Biotechnology

• Publication date

  2012-01-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1155/2012/586539PMID 22505815PMCID 3312296
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Thioredoxin

  2020cited by this paper
• Thioredoxin and glutaredoxin systems.

  2019cited by this paper
• Insights into Function, Catalytic Mechanism, and Fold Evolution of Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis*

  2010influential reference
• GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation.

  2008cited by this paper
• Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine.

  2008cited by this paper
• The methionine sulfoxide reductases: Catalysis and substrate specificities.

  2008cited by this paper
• Canonical sampling through velocity rescaling.

  2007cited by this paper
• NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus

  2007cited by this paper
• Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals.

  2007cited by this paper
• Maintenance of proteins and aging: The role of oxidized protein repair

  2006influential reference
• Oxidized protein degradation and repair in ageing and oxidative stress

  2006influential reference
• Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment

  2005cited by this paper
• Different Catalytic Mechanisms in Mammalian Selenocysteine- and Cysteine-Containing Methionine-R-Sulfoxide Reductases

  2005cited by this paper
• Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases.

  2005cited by this paper
• Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation.

  2005cited by this paper
• The enzymology and biochemistry of methionine sulfoxide reductases.

  2005cited by this paper
• Methionine oxidation and aging.

  2005cited by this paper
• Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage.

  2005cited by this paper
• Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival.

  2005cited by this paper
• Evidence for a New Sub-class of Methionine Sulfoxide Reductases B with an Alternative Thioredoxin Recognition Signature*

  2004cited by this paper
• A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force‐field parameter sets 53A5 and 53A6

  2004cited by this paper
• Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase.

  2004cited by this paper
• RefDB: A database of uniformly referenced protein chemical shifts

  2003cited by this paper
• Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases.

  2003influential reference
• Kinetic Characterization of the Chemical Steps Involved in the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis*

  2003cited by this paper
• High-quality life extension by the enzyme peptide methionine sulfoxide reductase

  2002influential reference
• Activity, tissue distribution and site‐directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1

  2002cited by this paper
• Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase

  2002cited by this paper
• Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function.

  2002cited by this paper
• Repair of Oxidized Proteins

  2001cited by this paper
• Reactive oxygen species: oxidative damage and pathogenesis

  1999cited by this paper
• Novel Selenoproteins Identified in Silico andin Vivo by Using a Conserved RNA Structural Motif*

  1999cited by this paper
• Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases.

  1999influential reference
• Peptide Folding: When Simulation Meets Experiment

  1999cited by this paper
• Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress.

  1998influential reference
• LINCS: A linear constraint solver for molecular simulations

  1997cited by this paper
• Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation.

  1997cited by this paper
• VMD: visual molecular dynamics.

  1996cited by this paper
• Oxidation of methionyl residues in proteins: tools, targets, and reversal.

  1995cited by this paper
• Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.

  1995cited by this paper
• Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.

  1995cited by this paper
• Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB

  1995cited by this paper
• Force field parametrization by weak coupling. Re-engineering SPC water

  1995cited by this paper
• Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.

  1995cited by this paper
• ICM—A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation

  1994cited by this paper
• Elucidating the folding problem of helical peptides using empirical parameters

  1994cited by this paper
• Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides

  1994cited by this paper
• Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

  1993cited by this paper
• Short protocols in molecular biology : a compendium of methods from Current protocols in molecular biology

  1989cited by this paper
• A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin.

  1989cited by this paper
• Thioredoxin.

  1985cited by this paper
• Molecular dynamics with coupling to an external bath

  1984cited by this paper
• Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli.

  1980cited by this paper

• Selenoproteins: Minute yet vital players governing cellular fate

  2025cites this paper
• Transcription factor KLF5 regulates MsrB1 to promote colorectal cancer progression by inhibiting ferroptosis through β-catenin.

  2025cites this paper
• Selenium metabolism and selenoproteins function in brain and encephalopathy

  2024cites this paper
• Physiological and Pathophysiological Roles of Thioredoxin Interacting Protein: A Perspective on Redox Inflammation and Metabolism

  2022cites this paper
• The Potential of a Protein Model Synthesized Absent of Methionine

  2022influential citation
• MsrB1 Promotes Proliferation and Invasion of Colorectal Cancer Cells via GSK-3β/β-catenin Signaling Axis

  2021cites this paper
• Thioredoxin-dependent system. Application of inhibitors

  2020cites this paper
• MICAL—methionine sulfoxide reductase couple: a new target for the development of neuroprotective strategies

  2014cites this paper
• Evolution of Structural and Coordination Features Within the Methionine Sulfoxide Reductase B Family

  2014cites this paper
• Selenoproteins: molecular pathways and physiological roles.

  2014cites this paper
• Direct Interaction of Selenoprotein R with Clusterin and Its Possible Role in Alzheimer’s Disease

  2013cites this paper
• Structure-functional Characterization of Mammalian Redox Proteins: Methionine sulfoxide reductase B1 (MsrB1), Glutaredoxin domain (Grx) of TGR, and Thioredoxin (Trx)

  2013cites this paper
• Cloning, Expression, and Characterization of a Methionine Sulfoxide Reductase B Gene from Nicotiana tabacum

  2013cites this paper
• Structural and biochemical insights into mammalian cobalt-substituted methionine sulfoxide reductase B1 using UV-visible spectroscopy and high-resolution NMR spectroscopy

  2012cites this paper