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Figure 6 | BMC Structural Biology

Figure 6

From: The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases

Figure 6

Superpositions of F o - F c electron density simulated annealing omit maps on refined ligands. The CoA moieties assume bent J-like conformations in the structures of MCLC and MCLR. Intramolecular hydrogen bonds between the adenosine rings and the pantetheine tails are indicated. A) Omit map at 2.5 σ for propionyl-CoA and oxalate bound in the active sites of the MCLC structure (PDB 4L80). The α-carbon of the propionyl moiety is in close proximity to oxalate (3.4 Å). B) Omit map at 2 σ for propionyl-CoA and glyoxylate modeled into one of the active sites of the MCLR structure (PDB 4L9Y). The α-carbon of the propionyl moiety is 3.7 Å from the carbonyl carbon of glyoxylate. C) Omit map at 2.0 σ for CoA and oxalate bound in six of the active sites in MCLR structure (PDB 4L9Z).

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