ArticleJournal of structural and functional genomics2014
Structural characterization of a hypothetical protein: a potential agent involved in trimethylamine metabolism in Catenulispora acidiphila.
Article in Journal of structural and functional genomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 7 citations in OpenAlex.
- Maize edible-legumes intercropping systems for enhancing agrobiodiversity and belowground ecosystem services.Scientific reports · 2024Article
- Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Design and Synthesis of Potent Quinazolines as Selective β-Glucocerebrosidase Modulators.Journal of medicinal chemistry · 2016Article
- Substrate-Induced Allosteric Change in the Quaternary Structure of the Spermidine N-Acetyltransferase SpeG.Journal of molecular biology · 2015Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci_0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci_0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci_0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.
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Registered trials
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