ArticleJournal of bacteriology2003
Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 72 citations in OpenAlex.
- Review
- A widespread group of large plasmids in methanotrophic Methanoperedens archaea.Nature communications · 2022Article
- Structural Insights into a Bifunctional Peptide Methionine Sulfoxide Reductase MsrA/B Fusion Protein fromAntioxidants (Basel, Switzerland) · 2021Article
- The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.Antioxidants (Basel, Switzerland) · 2018Review
- A Methionine Residue Promotes Hyperoxidation of the Catalytic Cysteine of Mouse Methionine Sulfoxide Reductase A.Biochemistry · 2016Article
- Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.The Journal of biological chemistry · 2015Article
- Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.PloS one · 2015Article
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.PloS one · 2015Article
- Multi-scale computational enzymology: enhancing our understanding of enzymatic catalysis.International journal of molecular sciences · 2013Review
- The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.Antioxidants & redox signaling · 2013Review
- Electrostatics of cysteine residues in proteins: parameterization and validation of a simple model.Proteins · 2012Article
- A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A.The Journal of biological chemistry · 2012Article
- Two highly homologous methionine sulfoxide reductase A from tomato (Solanum lycopersicum), exhibit distinct catalytic properties.The protein journal · 2012Article
- Methionine sulfoxide reductase A is a stereospecific methionine oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Redox proteomics of protein-bound methionine oxidation.Molecular & cellular proteomics : MCP · 2011Article
- Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.The Journal of biological chemistry · 2011Article
- Methionine sulfoxide reductase B (MsrB) of Mycobacterium smegmatis plays a limited role in resisting oxidative stress.Tuberculosis (Edinburgh, Scotland) · 2009Article
- Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae.Molecular microbiology · 2009Article
- Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae.The Journal of biological chemistry · 2009Article
- Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite.Molecular microbiology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections in humans results in the loss of their ability to colonize host cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic bacterium Mycobacterium tuberculosis refined to 1.5 A resolution. In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The structure reveals a methionine residue of one MsrA molecule bound at the active site of a neighboring molecule in the crystal lattice and thus serves as an excellent model for protein-bound methionine sulfoxide recognition and repair.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.