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![[Figure 1]](nj5323fig1mag.jpg)
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Figure 1
View of a typical PTE structure (PDB entry 1hzy; Benning et al., 2001  ). (a) The (β/α)8 TIM-barrel fold is shown as a cartoon, with helices in red, sheets in yellow, coils in green, the α-Zn2+ (buried) and β-Zn2+ (exposed) ions as magenta spheres and a single bridging water shown as a cyan sphere. The six residues that bind to the two Zn2+ ions are shown as stick representations, with C atoms colored yellow, N atoms blue and O atoms red. The N- and C-terminal residues are labeled N and C, respectively. (b) Close-up view of the active site of the apo PTE structure. The buried α-Zn2+ ion is directly bound to His55, His57 and Asp301, while the exposed β-Zn2+ ion is bound to His201 and His230. The carbamate functional group bound to Lys169 interacts with both Zn2+ ions. Coloring is as in (a). |
![[Figure 1]](nj5323fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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