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. 2003 May 15;22(10):2334–2347. doi: 10.1093/emboj/cdg244

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Fig. 4. 12S domains. (A) Stereo view superposition of 12S domains: N-terminal domain 1 in blue and C-terminal domain 2 in red. (B) Structure-based sequence alignment of 12S domains 1 (Dom1) and 2 (Dom2), 4-chlorobenzoyl-CoA dehalogenase (PDBid 1NZY), MMCoA decarboxylase from E.coli (PDBid 1EF8 and 1EF9), rat enoyl-CoA hydratase (PDBid 2DUB) and rat dienoyl-CoA isomerase (PDBid 1DCI), with 12S sequence numbers and secondary structure. Residues in the other proteins in structural elements conserved in 12S are in green; amino acids conserved with 12S are underlined. Adenine- and CoA-binding residues are boxed in green and purple, respectively. Amino acids that are reversed relative to the standard CoA-binding motif are boxed in brown. (C) Stereo view superposition of 12S domain 1 (blue) with MMCoA decarboxylase from E.coli (PDB code 1EF9) (black). 12S-bound MMCoA is in space-filling representation.