Volume 15, Issue 7, Pages (July 2007)

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Volume 15, Issue 7, Pages 853-861 (July 2007) Crystallographic Snapshots of Oxalyl-CoA Decarboxylase Give Insights into Catalysis by Nonoxidative ThDP-Dependent Decarboxylases  Catrine L. Berthold, Cory G. Toyota, Patricia Moussatche, Martin D. Wood, Finian Leeper, Nigel G.J. Richards, Ylva Lindqvist  Structure  Volume 15, Issue 7, Pages 853-861 (July 2007) DOI: 10.1016/j.str.2007.06.001 Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 1 ThDP Catalysis in Oxalyl-CoA Decarboxylation 1, ThDP-ylid; 2, oxalyl-CoA; 3, predecarboxylation intermediate; 4, α-carbanion/enamine intermediate; 5, formyl-CoA-ThDP covalent complex; 6, formyl-CoA. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 2 OXC in Complex with Oxalyl-CoA (A) The OXC tetramer represented with one of the catalytic dimers in a surface mode. dzThDP, ADP, and oxalyl-CoA are represented as balls-and-sticks. The C-terminal organizing upon substrate binding is shown in red. (B) The substrate binding site with side chains interacting with oxalyl-CoA shown as sticks. Dashed blue lines are hydrogen bonds and red spheres represent water molecules. The C-terminal residues after Arg-555 have been omitted for clarity. The main chain of two residues in the newly organized C terminus is shown colored in red. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 3 View of the Active Site (A) Close-up of oxalyl binding. (B) Structure of the postdecarboxylation intermediate. (C) Structure of the product complex. For all images, the C terminus after residue Arg-555 has been omitted for clarity. Residues from different subunits are colored differently and red spheres represent water molecules. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 4 Annealed Composite Omit Maps Annealed composite omit maps calculated for the structures shown around the active site in (A) the oxalyl-CoA complex, (B) the postdecarboxylation intermediate complex, and (C) the product complex. The contour level is 1σ. For labeling of residues see Figure 3. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 5 Postdecarboxylation Intermediates—4 and 5 in Figure 1—Viewed along the Thiazolium Plane Grey carbons represent the nonplanar protonated intermediate (5), and the enamine carbanion form (4) is shown with carbons in cyan. Both intermediates have been refined with the covalent postdecarboxylation complex data. The annealed composite omit map is contoured at 1σ and shows a better fit for the protonated intermediate. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 6 Stereo View of the Aligned Structures The substrate, intermediate, and product complexes are colored green, pink, and blue, respectively. Water molecules of the three structures are colored the same but in a lighter shade. The C terminus after residue Arg-555 has been omitted for clarity. Structure 2007 15, 853-861DOI: (10.1016/j.str.2007.06.001) Copyright © 2007 Elsevier Ltd Terms and Conditions