Analyzing the symmetrical arrangement of structural repeats in proteins with CE-Symm
Fig 4
A) Internal C2 symmetry in one chain of a MaoC domain protein dehydratase from Chloroflexus aurantiacus (4E3E) displaying a “double hot dog” fold. B) Full trimeric assembly, with the six individual hot dog domains colored. The quaternary structure has a threefold cyclic symmetry that combines with the twofold internal symmetry into a dihedral D3 symmetry equivalent to the quaternary structure of homologs without the internal domain duplication. C) Sequence alignment showing that the catalytic R/N-####-H motif (yellow) is lost in the first domain but retained in the second. Amino acid identity is shown in blue and similarity in magenta.