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![[Figure 3]](yt5023fig3mag.jpg)
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Figure 3
(a) Ribbon diagram of H(P)PR generated from the refined crystal structure. The monomer located in the asymmetric unit is depicted. Secondary-structure elements were assigned with the program PROMOTIF (Hutchinson & Thornton, 1996  ). The structure contains two domains: the lower portion is the cosubstrate-binding domain and the upper portion is the catalytic or substrate-binding domain. β-Strands are shown as green arrows and helices are shown in red. (b) The topology diagram generated with TOPS (https://www.tops.leeds.ac.uk) shows the two-domain enzyme, with the larger domain consisting of a seven-stranded β-sheet with Rossmann-fold topology that forms the cosubstrate-binding domain. The smaller domain is represented by a five-stranded β-sheet and forms the substrate-binding domain. Strands are depicted as green triangles and helices as red spheres. (c) View of the H(P)PR dimer approximately along the twofold rotation axis. The dimer interface is mainly composed of residues from the cosubstrate-binding domains. |
![[Figure 3]](yt5023fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
