 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 5]](xb5072fig5mag.jpg)
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Figure 5
(a) The secondary and tertiary structure of BcCCP. A ribbon diagram of subunit A showing α-helices coloured magenta and β-strands coloured orange, with Zn2+ depicted as a grey sphere. The N- and C-terminal positions are labelled, as are the α-helices and β-strands. A small section of a loop (residues 157 and 158, marked with black asterisks), as well as the first and last residues at the N- and C-termini, are absent from the model owing to disorder. (b) The primary and secondary structure of BcCCP. Residues that are strictly or highly conserved in BcCCP, BmCCP, SdCCP, PaCCP and CeCCPP-6 are shown on black and grey backgrounds, respectively. Three residues that coordinate Zn2+ are marked with yellow stars. The three motifs of the N-terminal domain which are conserved in CCP members are enclosed by green boxes. |
![[Figure 5]](xb5072fig5.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
