ArticleActa crystallographica. Section F, Structural biology communications2018
Solution NMR structures of oxidized and reduced Ehrlichia chaffeensis thioredoxin: NMR-invisible structure owing to backbone dynamics.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Trp31 Residue of Trx-1 Is Essential for Maintaining Antioxidant Activity and Cellular Redox Defense Against Oxidative Stress.Antioxidants (Basel, Switzerland) · 2025Article
- Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of action.PLoS pathogens · 2024Article
- The Thioredoxin System of Mammalian Cells and Its Modulators.Biomedicines · 2022Review
- Solution structure for an Encephalitozoon cuniculi adrenodoxin-like protein in the oxidized state.Protein science : a publication of the Protein Society · 2020Article
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4 authors at 3 institutions in 1 country.
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Abstract
Thioredoxins are small ubiquitous proteins that participate in a diverse variety of redox reactions via the reversible oxidation of two cysteine thiol groups in a structurally conserved active site. Here, the NMR solution structures of a reduced and oxidized thioredoxin from Ehrlichia chaffeensis (Ec-Trx, ECH_0218), the etiological agent responsible for human monocytic ehrlichiosis, are described. The overall topology of the calculated structures is similar in both redox states and is similar to those of other thioredoxins: a five-stranded, mixed β-sheet (β1-β3-β2-β4-β5) surrounded by four α-helices. Unlike other thioredoxins studied by NMR in both redox states, the
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