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![[Figure 1]](be5117fig1mag.jpg)
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Figure 1
Sequence alignment of KHKs and related proteins based on observed secondary structure. Regions in which the secondary structures are conserved throughout all five members of the ribokinase family are shown above the sequences. The numbering system used to denote the secondary structure is based on that of KHK-A. The alternatively spliced region that differs between the KHK-A and KHK-C isoforms is highlighted in red in the KHK-C sequence. There are additional strands and helices in ecRK, hsAK and tgAk, but the overall topologies of the structures are similar to that of KHK. The residues that make interactions with the substrates are shown in green. The mutated residues Gly40 and Ala43 are boxed in purple and completely conserved residues are highlighted in blue. The highly conserved `GG' and `DTXGAGD' motifs are underlined in orange. Val49, which is coloured yellow, represents the site of a polymorphic variant (V/I) of KHK (Bonthron et al., 1994  ). The sequences in the table are KHK-A, Homo sapiens ketohexokinase KHK-A (Swiss-Prot P50053); KHK-C, H. sapiens ketohexokinase KHK-C (Swiss-Prot P50053-2); ecRK, E. coli ribokinase (Swiss-Prot P0A9J6; PDB code 1rkd; Sigrell et al., 1998); hsAK, H. sapiens adenosine kinase (Swiss-Prot P55263; PDB code 1bx4; Mathews et al., 1998); tgAK, Toxoplasma gondii adenosine kinase (Swiss-Prot Q9TVW2; PDB code 1lii; Schumacher et al., 2000). Sequence alignment was carried out using the program Jalview (Clamp et al., 2004). |
![[Figure 1]](be5117fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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