Structural and Biochemical Studies of Human 4-hydroxy-2-oxoglutarate Aldolase: Implications for Hydroxyproline Metabolism in Primary Hyperoxaluria
Figure 7
Structural comparisons between hHOGA and E. coli DHDPS.
(A) Superposition of hHOGA and E. coli DHDPS (PDB ID: 3DUO) pyruvate-bound active sites (RMSD = 0.19 Å for Cα atoms) [28]. hHOGA coloring is the same as in Fig. 6. DHDPS carbon atoms are colored in pale cyan and cyan (adjacent subunit). Carbon atoms for pyruvate bound to DHDPS are colored gray. Hydrogen bonds are shown using dashed lines for hHOGA (gray) and DHDPS (blue). Amino acid residues for the two enzymes are indicated in the following order: hHOGA/DHDPS. (B) Model of the HOG•hHOGA complex. HOG carbon atoms and putative hydrogen bonds to hHOGA are colored yellow (R-form) and cyan (S-form).