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Figure 2 | BMC Structural Biology

Figure 2

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 2

Neighbor Joining Tree of the CitE-like superfamily of enzymes. Canonical malate synthases of E. coli (MSG and MSA) serve as outgroup. Green stars represent crystal structures that were solved during this study. Yellow stars represent publically available structures of CitE-like enzymes and malate synthases (see Table 1). No structures are available for the true β-subunit of the ATP-independent citrate lyase (CitE). All types of known malyl-CoA lyases belong to phylogenitically distinct clusters, respectively. The malyl-CoA thioesterase of R. sphaeroides is also member of a separate sub-group of enzymes. Haloarchaeal malate synthase (HaloMS) is closely related to enzymes that constitute the haloarchaeal form of a malyl-CoA lyase (HaloMCL). The scale bar corresponds to the number of amino acid substitutions per site.

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