ArticleBiochemistry2012
Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- A Bacterial Inflammation Sensor Regulates c-di-GMP Signaling, Adhesion, and Biofilm Formation.mBio · 2021Article
- A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target inFrontiers in veterinary science · 2020Article
- The role of peroxiredoxins in cancer.Molecular and clinical oncology · 2017Article
- Peroxiredoxin Catalysis at Atomic Resolution.Structure (London, England : 1993) · 2016Article
- Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.Trends in biochemical sciences · 2015Review
- Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs.Protein science : a publication of the Protein Society · 2015Article
- Tuning of peroxiredoxin catalysis for various physiological roles.Biochemistry · 2014Review
- Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus.Biochemistry · 2014Article
- The quality and validation of structures from structural genomics.Methods in molecular biology (Clifton, N.J.) · 2014Article
- The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin.Biochemistry · 2013Article
- Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination.The FEBS journal · 2013Review
- Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Kinetic analysis of the interactions between plant thioredoxin and target proteins.Frontiers in plant science · 2013Article
- Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.Methods in enzymology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxiredoxins (Prx) make up a family of enzymes that reduce peroxides using a peroxidatic cysteine residue; among these, members of the PrxQ subfamily are proposed to be the most ancestral-like yet are among the least characterized. In many PrxQ enzymes, a second "resolving" cysteine is located five residues downstream from the peroxidatic Cys, and these residues form a disulfide during the catalytic cycle. Here, we describe three hyperthermophilic PrxQ crystal structures originally determined by the RIKEN structural genomics group. We reprocessed the diffraction data and conducted further refinement to yield models with R(free) values lowered by 2.3-7.2% and resolution extended by 0.2-0.3 Å, making one, at 1.4 Å, one of the best resolved peroxiredoxins to date. Comparisons of two matched thiol and disulfide forms reveal that the active site conformational change required for disulfide formation involves a transition of ~20 residues from a pair of α-helices to a β-hairpin and 3(10)-helix. Each conformation has ~10 residues with a high level of disorder providing slack that allows the dramatic shift, and the two conformations are anchored to the protein core by distinct nonpolar side chains that fill three hydrophobic pockets. Sequence conservation patterns confirm the importance of these and a few additional residues for function. From a broader perspective, this study raises the provocative question of how to make use of the valuable information in the Protein Data Bank generated by structural genomics projects but not described in the literature, perhaps remaining unrecognized and certainly underutilized.
Indexed as
Identifiers
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.