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. Author manuscript; available in PMC: 2012 Aug 2.
Published in final edited form as: Biochemistry. 2011 Jul 5;50(30):6539–6548. doi: 10.1021/bi200632j

Figure 2.

Figure 2

A. Sequence alignment of structurally characterized acyltransferases (AT). DSZS AT, S. coelicolor and E. coli acyltransferases (MAT) are malonyl-specific enzymes, whereas the two ATs from the 6-deoxyerythronolide B synthase (DEBS) are methylmalonyl-specific. Sequences were aligned with ClustalW2 [33]. The formatted figure of aligned sequences was generated using ESPript [34]. Secondary structures of DSZS AT (top) and E. coli MAT (bottom) are annotated. Similar and strictly conserved residues are indicated by red letters and red boxes respectively. The catalytic motif GHSXG is present in all sequences. The missing gap in sequence alignment is due to an extra C-terminal β-sheet in the DEBS ATs. B. Structural alignment of DSZS AT (green) and S. coelicolor MAT (1NM2 [10], red). C-terminal secondary structural elements of S. coelicolor MAT, which are absent in DSZS AT, are labeled. Differences in β-sheets arrangements can also be observed (arrow). C. Alignment of DSZS AT (green) and DEBS AT5 domain (2HG4 [12], purple).