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. Author manuscript; available in PMC: 2019 Dec 11.
Published in final edited form as: Biochemistry. 2019 Nov 26;58(49):4970–4982. doi: 10.1021/acs.biochem.9b00878

Figure 2.

Figure 2.

D. radiodurans DXP synthase in the (A and C) predecarboxylation and (B and D) postdecarboxylation states illustrating the conformational change of the fork (teal, unresolved in the open structure) and spoon (orange) regions from the closed PLThDP-bound structure to the open postdecarboxylation (shown as the enamine) structure. (C) Interactions of H51 and H304 (E. coli DXP synthase H49 and H299, respectively) with the phosphonyl moiety of PLThDP (and, by extension, the carboxyl moiety of LThDP) in the closed conformation. (D) Movement of the spoon and fork motifs away from the active site in the open conformation removes H304 from the active site. Prepared in UCSF Chimera.