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Figure 2
The structure of WcbI reveals a novel fold. (a) Cartoon representation of the crystal structure of WcbI in two orientations. Termini and secondary-structure elements are labelled. For the N-terminal subdomain α-helices and loops are shown in red and β-sheets in yellow; for the C-terminal subdomain α-helices and loops are shown in blue and β-sheets in green. (b) Stereoview of the Cα backbone in the same orientation as in the left-hand image of (a). Every tenth residue is numbered. (c) Topological diagram of the polypeptide fold with α-helices indicated by circles and β-strands by triangles coloured as in (a). (d) Cartoon representation of WcbI in the orientations in (a) coloured as a rainbow with the N-terminus in blue and the C-terminus in red. (e) Schematic diagram of the fold of WcbI. α-Helices and 310-helices are shown as cylinders and β-sheets are shown as arrows. Secondary-structure elements are coloured as in (d). The start and end residue of each element is indicated. (f) Cartoon representation of the novel fold C-terminal subdomain coloured as a rainbow with the N-terminus in blue and the C-terminus in red. The substrate coenzyme A is shown as spheres. Carbon, cyan; oxygen, red; nitrogen, blue; sulfur, yellow; phosphorus, orange. Interacting residues from the novel subdomain are shown as lines. The secondary-structure assignments in all panels were made according to TOPS (Michalopoulos et al., 2003BB33). (a), (b), (d) and (f) were prepared with the PyMOL Molecular Graphics System (Schrödinger) and (c) was prepared with TOPS.

IUCrJ
Volume 1| Part 1| January 2014| Pages 28-38
ISSN: 2052-2525
https://doi.org/10.1107/S205225251302695X