Figure 3.
Fig. 3. Fold, topology, and sequence of E. coli MECP
synthase. (a) Stereo C trace
color-ramped from blue (N terminus) to red (C terminus). Every
10th C is depicted
by a black sphere and labeled. (b and c) Ribbon and topology
diagrams of a monomer ( -sheet,
purple; -helix,
gold; -helix,
red). (d) Sequence alignment of MECP synthase from E. coli, M.
tuberculosis, and part of the P. falciparum protein. The
secondary structure elements based on the E. coli enzyme
structure are colored and labeled as in b. Residues whose
identity is strictly conserved in all three sequences are boxed
in black, conservative substitutions in gray, gray triangles
mark Zn2+ ligands, and an open triangle the Mn2+-binding
Glu-135. Circles mark CDP-binding residues (open and filled to
distinguish subunits).
trace
color-ramped from blue (N terminus) to red (C terminus). Every
10th C 
-sheet,
purple; 
-helix,
red). (d) Sequence alignment of MECP synthase from E. coli, M.
tuberculosis, and part of the P. falciparum protein. The
secondary structure elements based on the E. coli enzyme
structure are colored and labeled as in b. Residues whose
identity is strictly conserved in all three sequences are boxed
in black, conservative substitutions in gray, gray triangles
mark Zn2+ ligands, and an open triangle the Mn2+-binding
Glu-135. Circles mark CDP-binding residues (open and filled to
distinguish subunits).