Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways
Fig 4
RLM protein phosphatases arose multiple times in evolution.
Cartoon depictions are labeled at the termini. (A) HAD domain-like phosphatase (pink cartoon) adopts the parallel β-strand topology order indicated below and binds Mg2+ cofactor (green sphere) using the active site motif (magenta) from the RLM (rainbow). (B) PGM phosphatases (light blue cartoon) adopt the mixed β-strand topology order indicated below and catalyze metal-independent hydrolysis using a composite active site motif (magenta) that is both within and outside of the RLM (rainbow). Flavodoxin-like protein phosphatases (light orange cartoon, rainbow RLM, and magenta active site) fall into different ECOD T-groups with the typical flavodoxin-like β-strand order indicated below. The * denotes alternate T-group topologies for β-strand 5 (missing in panel C, permuted and antiparallel in panel D, and permuted in panel E). (C) Phosphotyrosine protein phosphatases I-like (D) (Phosphotyrosine protein) phosphatases II (E) rhodanese/cell cycle control phosphatase.