Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways
Fig 7
Diverse binding modes of inorganic metal cofactors.
RLM SSEs are colored in rainbow with yellow crossover loop and magenta catalytic loop. (A) Mg2+ (green sphere) bound to 4-methyl-5-beta-hydroxyethylthiazole kinase (PDB: 1ESQ) Rossmann-like X-group domain (slate cartoon) coordinates ATP substrate (black stick, colored by element). (B) Mg2+ (green sphere) bound to shikimate kinase (PDB: 2SHK) P-loop domains-like X-group (pink cartoon) coordinates ADP (black stick, colored by element). (C) Mg2+ (green sphere) bound to sphingosine kinase (PDB: 3VZD) flavodoxin-like X-group domain (green cartoon) coordinates pyrophosphate (orange stick). (D) Ni2+ bound to trimer of ornithine transcarbamylase (PDB: 2W37) Rossmann-like X-group domain (slate cartoon) mediates trimerization (white and gray cartoon chains) through coordinating residues (stick). (E) MnmE G-domain (PDB: 2GJ8) from P-loop domains-like X-group (pink cartoon) binds K+ (violet sphere) near the transition state analog Mg2+ (green sphere)-GDP-AlF (black stick, colored by element). (F) Co2+ (pink spheres) bound to active site of cobalt-activated peptidase TET1 (PDB: 2CF4) phosphorylase/hydrolase-like X-group domain (wheat cartoon).