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Figure 8 | BMC Biochemistry

Figure 8

From: The mononuclear metal center of type-I dihydroorotase from aquifex aeolicus

Figure 8

DHO multiple sequence alignment. The amino acid sequence of A. aeolicus (Aa), S. aureus (Sa), E. coli (Ec) and the DHO domain of human CAD (Hu) were aligned using Clustral W (ExPays Proteomics Site). The A. aeolicus residues that are conserved in S. aureus, E. coli and CAD are shaded gray. The α- and β-site Zn ligands are shown in white lettering on a black background. All of these residues are conserved and aligned with the exception of the active site ligand Asp153 in A. aeolicus. This residue is conserved in S. aureus DHO, but in E. coli and CAD, it is a Lys (Lys102 in E. coli), which is carboxylated and bridges the two zinc ions. The Lys is shifted upstream relative to the Asp in A. aeolicus and S. aureus. In a previous pair wise alignment [3] this lysine occupies the same position in the E. coli and CAD sequences.

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