Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways
Fig 3
Heterogeneous reactions catalyzed by the Rhodanese F-group (EC numbers in bold) through Cys residue intermediates: (A) Rhodanese reactions transfer sulfur groups from thiosulfate to cyanide (EC: 2.8.1.1) or from mercaptopyruvate to oxidize thioredoxin (EC: 2.8.1.2). (B) GlpE rhodanese domain from PDB: 1GMX (gray cartoon) with RLM (rainbow) and active site with an additional conserved motif (magenta stick). (C) Sulfur group transfer to the C-terminal ampylated Gly residue of sulfur carrier protein (SCP) in a bi-functional MOCS3 (Molybdenum Cofactor Synthesis 3) enzyme (EC: 2.8.1.11 and EC: 2.7.7.80). (D) CDC25 phosphate hydrolysis from protein Phospho-Tyr residue (EC: 3.1.3.48). (E) CDC25 phosphatase rhodanese-like domain from PDB: 1QB0 with RLM domain (rainbow) retains similar active site (magenta stick). (B, E) Note that the β-strand (β2; green) can be considered as being barely existent (or vestigial) among the universe of RLMs being considered in this work.