Thioredoxin and peptide methionine sulfoxide reductase: Convergence of similar structure and function in distinct structural folds

Автор: Gladyshev Vadim N.
Журнал: Proteins
Том: 46
Номер: 2
Год издания: 2002
Первая страница: 149
Последняя страница: 152
DOI: 10.1002/prot.10003
Аннотация: Thioredoxin (Trx) and peptide methionine sulfoxide reductase (PMSR) are small thiol oxidoreductases implicated in antioxidant defense and redox regulation of cellular processes. Here we show that the structures of Trx and PMSR exhibit resemblance in their αβ core regions and that the active site cysteines in two proteins occupy equivalent positions downstream of a central β‐strand and at the N‐terminus of an α‐helix. Moreover, we identified a PMSR subfamily that contains an active site CxxC motif (two cysteines separated by two other amino acids) positioned similarly to the catalytic redox active CxxC motif in Trx. However, Trx and PMSR are characterized by distinct ancient folds that differ in both orientation of secondary structures and their patterns. Trx is a member of the Trx‐fold superfamily, whereas PMSR has a unique fold not found in other proteins. The data suggest that similar structures and functions of Trx and PMSR were acquired independently during evolution and point to a general strategy of identifying new redox regulatory proteins.
Добавил в систему: Гладышев Вадим Николаевич

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