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![[Figure 2]](cb5114fig2mag.jpg)
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Figure 2
Overall structure of the VcCMAS enzyme. (a) Cartoon representation of the apo VcCMAS dimer. Each subunit is colored as a rainbow. CMP-sialic acid is modeled in the active site. The helices and β-strands mentioned in the text are labeled. (b) The electrostatic surface potential map of the apo structure highlights the open conformation of the enzyme. The negatively charged regions are colored red, neutral regions white and positively charged regions blue. (c) Cartoon representation of the CDP-bound VcCMAS tetramer observed in the asymmetric unit. The four subunits are colored blue, pink, green and cyan and are labeled A, B, C and D. The CDP present in the active site is shown in stick representation. (d) The electrostatic surface potential map of the CDP-bound structure shows the `partially closed' conformation of the enzyme. |
![[Figure 2]](cb5114fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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