{
  "abstract": "Tryparedoxin (TryX) is a member of the thioredoxin (TrX) fold family involved in the regulation of oxidative stress in parasitic trypanosomatids. Like TrX, TryX carries a characteristic Trp-Cys-Xaa-Xaa-Cys motif, which positions a redox-active disulfide underneath a tryptophan lid. We report the structure of a Crithidia fasciculata tryparedoxin isoform (CfTryX2) in two crystal forms and compare them with structures determined previously. Efforts to chemically generate crystals of reduced TryX1 were unsuccessful, and we carried out a novel experiment to break the redox-active disulfide, formed between Cys-40 and Cys-43, utilizing the intense x-radiation from a third generation synchrotron undulator beamline. A time course study of the S-S bond cleavage is reported with the structure of a TryX1 C43A mutant as the control. When freed from the constraints of a disulfide link to Cys-43, Cys-40 pivots to become slightly more solvent-accessible. In addition, we have determined the structure of Trypanosoma brucei TryX, which, influenced by the molecular packing in the crystal lattice, displays a significantly different orientation of the active site tryptophan lid. This structural change may be of functional significance when TryX interacts with tryparedoxin peroxidase, the final protein in the trypanothione-dependent peroxidase pathway. Comparisons with chloroplast TrX and its substrate fructose 1,6-bisphosphate phosphatase suggest that this movement may represent a general feature of redox regulation in the trypanothione and thioredoxin peroxidase pathways.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "Magnus Alphey"
    },
    {
      "name": "Mads Gabrielsen"
    },
    {
      "name": "Elena Micossi"
    },
    {
      "name": "Gordon Leonard"
    },
    {
      "name": "Sean Mcsweeney"
    },
    {
      "name": "Raimond B.G. Ravelli"
    },
    {
      "name": "Emmanuel Tetaud"
    },
    {
      "name": "Alan Fairlamb"
    },
    {
      "name": "Charles Bond"
    },
    {
      "name": "William Hunter"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/50db9tmqspb6e.bib",
  "cited_by": 47,
  "doi": "10.1074/jbc.m301526200",
  "fulltext_url": null,
  "id": "50db9tmqspb6e",
  "issns": [
    "0021-9258",
    "1083-351X"
  ],
  "landing_url": "https://hal.science/hal-05753745v1",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1312|Redox biology and oxidative stress"
    ]
  ],
  "openalex": "W2120023357",
  "pdf_url": "http://www.jbc.org/article/S0021925819751163/pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-17",
  "publisher": "American Society for Biochemistry and Molecular Biology",
  "ris": "https://research.draconitic.com/paper/50db9tmqspb6e.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:36Z",
      "native_id": "hal-05753745",
      "source": "hal",
      "url": "https://hal.science/hal-05753745v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Redox biology and oxidative stress",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei",
  "title_text": "Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:36Z",
  "url": "https://research.draconitic.com/paper/50db9tmqspb6e",
  "venue": "Journal of Biological Chemistry",
  "versions": []
}