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Figure 5 | BMC Structural Biology

Figure 5

From: Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G

Figure 5

SSM overlay of MSA [PDB: 3CV2], MSG [PDB: 1P7T], and MSH [PDB: 3OYZ] pyruvate/Acetyl-CoA ternary complexes. a) Stereoview of the N-terminal regions: MSA 10-412, MSG 4-585 and MSH 5-284 rendered in red, blue and green respectively. Ends of protein chains are labeled with residue numbers except MSH residue 5 which is marked by an asterisk at the center of the image. View is from the bottom of the TIM barrel, opposite the active site; C-terminal domains are not shown for clarity. b) Overlay as in part a, but only showing the C-terminal domains of each protein: MSA 412-533, MSG 585-722, and MSH 328-432. The active site base Asp 388 in MSH is shown (center) in stick form with carbon atoms colored yellow and corresponds to the same position as Asp 447 in MSA and Asp 631 in MSG (within 0.7 and 1.0 Å respectively). Disordered loop in MSH is shown as a green dotted line. c) Overlay as in parts a and b, but only showing extreme C-terminal regions: MSA 463-533, MSG 647-722, and MSH 404-432. Helix 2 refers to the second helix of the C-terminal domain which immediately follows the active site aspartate residue as seen in figure 5b.

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