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![[Figure 2]](mh5163fig2mag.jpg)
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Figure 2
Multiple sequence alignment of related hydrolase domains of 10-formyltetrahydrofolate dehydrogenase and other folate-utilizing proteins. The sequences of various folate-utilizing proteins are aligned with that of zNt-FDH (Zf_Nt-FDH) to ascertain the similarities of their amino-acid sequences. The aligned proteins include Nt-FDH from Rattus norvegicus (Rn_Nt-FDH; Chumanevich et al., 2004  ), Nt-FDH from Homo sapiens (Hs_Nt-FDH; Kursula et al., 2006), FMT from E. coli (Ec_FMT; Schmitt et al., 1996), ArnA-TF from E. coli (Ec_ArnA-TF; Gatzeva-Topalova et al., 2005) and GART from Symbiobacterium toebii (St_GART; Yoshizawa et al., 2011). The completely conserved residues are shown on a red background. The residues of zNt-FDH involved in ligand binding via hydrogen bonds, according to the protein structures of the 10-FDDF and THF complexes, are marked by stars and squares, respectively. The green box indicates the highly conserved region with the HxSLLPxxxG sequence motif. The sequence alignment was performed with STRAP and ClustalW. The secondary-structure elements of Zf_Nt-FDH were calculated with ESPript (https://espript.ibcp.fr) and are presented at the top of the sequences. |
![[Figure 2]](mh5163fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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