ArticleMolecular microbiology2009
Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae.
Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- Where metabolism and virulence meet-sulfoxide reductases as determinants of bacterial survival.Biochemical Society transactions · 2026Review
- Role of ClpX and MsrA/B in the Oxidative and Cell Wall Stress Response in Bacillus anthracis Sterne.MicrobiologyOpen · 2026Article
- Novel Insights into the Molecular Mechanisms Underlying Robustness and Stability in Probiotic Bifidobacteria.Applied and environmental microbiology · 2023Article
- The oxidative stress response ofFrontiers in microbiology · 2023Review
- The Peptide Methionine Sulfoxide Reductase (MsrAB) ofAntioxidants (Basel, Switzerland) · 2022Article
- A Novel Small RNA, DsrO, in Deinococcus radiodurans Promotes Methionine Sulfoxide Reductase (Applied and environmental microbiology · 2022Article
- Catechin Mediates Ferroptosis to Exert an Anti-Inflammatory Effect on RAW 264.7 Cells.Foods (Basel, Switzerland) · 2022Article
- Progress toward automated methyl assignments for methyl-TROSY applications.Structure (London, England : 1993) · 2022Article
- Structural Insights into a Bifunctional Peptide Methionine Sulfoxide Reductase MsrA/B Fusion Protein fromAntioxidants (Basel, Switzerland) · 2021Article
- REDCRAFT: A computational platform using residual dipolar coupling NMR data for determining structures of perdeuterated proteins in solution.PLoS computational biology · 2021Article
- Sulfoxide Reductases and Applications in Biocatalytic Preparation of Chiral Sulfoxides: A Mini-Review.Frontiers in chemistry · 2021Review
- Article
- A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress.PloS one · 2018Article
- Protein structure refinement using a quantum mechanics-based chemical shielding predictor.Chemical science · 2017Article
- Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.EMBO reports · 2016Article
- A community resource of experimental data for NMR / X-ray crystal structure pairs.Protein science : a publication of the Protein Society · 2016Review
- Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance.Applied and environmental microbiology · 2015Article
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.PloS one · 2015Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- Experimental evidence validating the computational inference of functional associations from gene fusion events: a critical survey.Briefings in bioinformatics · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methionine sulphoxide reductases (Msr) catalyse the reduction of oxidized methionine to methionine. These enzymes are divided into two classes, MsrA and MsrB, according to substrate specificity. Although most MsrA and MsrB exist as separate enzymes, in some bacteria these two enzymes are fused to form a single polypeptide (MsrAB). Here, we report the first crystal structure of MsrAB from Streptococcus pneumoniae (SpMsrAB) at 2.4 A resolution. SpMsrAB consists of an N-terminal MsrA domain, a C-terminal MsrB domain and a linker. The linker is composed of 13 residues and contains one 3(10)-helix and several hydrogen bonds interacting with both MsrA and MsrB domains. Interestingly, our structure includes the MsrB domain complexed with an SHMAEI hexa-peptide that is the N-terminal region of neighbouring MsrA domain. A kinetic analysis showed that the apparent K(m) of SpMsrAB for the R-form-substrate was 20-fold lower than that for the S-form substrate, indicating that the MsrB domain had a much higher affinity for the substrate than the MsrA domain. Our study reveals the first structure of the MsrAB by providing insights into the formation of a disulphide bridge in the MsrB, the structure of the linker region, and the distinct structural nature of active site of each MsrA and MsrB domain.
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