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• W2001755249 endingPage "e1000541" @default.
• W2001755249 startingPage "e1000541" @default.
• W2001755249 abstract "The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the variation in catalytic machinery of Trx fold proteins is essential in providing a foundation for understanding their functional diversity and predicting the function of the many uncharacterized members of the class. The proteins of the Trx fold class retain common features—including variations on a dithiol CxxC active site motif—that lead to delivery of function. We use protein similarity networks to guide an analysis of how structural and sequence motifs track with catalytic function and taxonomic categories for 4,082 representative sequences spanning the known superfamilies of the Trx fold. Domain structure in the fold class is varied and modular, with 2.8% of sequences containing more than one Trx fold domain. Most member proteins are bacterial. The fold class exhibits many modifications to the CxxC active site motif—only 56.8% of proteins have both cysteines, and no functional groupings have absolute conservation of the expected catalytic motif. Only a small fraction of Trx fold sequences have been functionally characterized. This work provides a global view of the complex distribution of domains and catalytic machinery throughout the fold class, showing that each superfamily contains remnants of the CxxC active site. The unifying context provided by this work can guide the comparison of members of different Trx fold superfamilies to gain insight about their structure-function relationships, illustrated here with the thioredoxins and peroxiredoxins." @default.
• W2001755249 created "2016-06-24" @default.
• W2001755249 creator A5020002876 @default.
• W2001755249 creator A5078018356 @default.
• W2001755249 date "2009-10-23" @default.
• W2001755249 modified "2023-10-16" @default.
• W2001755249 title "An Atlas of the Thioredoxin Fold Class Reveals the Complexity of Function-Enabling Adaptations" @default.
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• W2001755249 doi "https://doi.org/10.1371/journal.pcbi.1000541" @default.
• W2001755249 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2757866" @default.
• W2001755249 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19851441" @default.
• W2001755249 hasPublicationYear "2009" @default.
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