An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.

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

SUBMITTER: Atkinson HJ 

PROVIDER: S-EPMC2757866 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature