Fig. 5
From: New insights into the nutritional genomics of adult-onset riboflavin-responsive diseases
Riboflavin-responsive mutants of MTHFR. The alignment was generated for known (or predicted) MTHFR sequences from human (Homo sapiens NP_005948.3), pig (Sus scrofa, XP_005665053.1), mouse (Mus musculus, AAD20313.1), frog (Xenopus laevis, XP_018083188.1), worm (Caenorhabditis elegans, Q17693.2), nematode (Trichinella pseudospiralis KRZ29695.1), fruit fly (Drosophila melanogaster, NP_648462.1), fungus (Candida auris, GBL48066.1), yeast (Saccharomyces cerevisiae, KAF4004889.1) and bacteria (Pseudomonadota, WP_000007523.1) using ClustalX version 2.1 [113]. Amino acid numbers for the human sequence are indicated. The red box indicates the location of Ala222. B A ribbon diagram (generated in VMD 1.9.1) [114] of the MTHFR crystal structure in complex with FAD (white) is shown. [72] Ala222 (yellow) lies at the C-terminal end of the a6 helix. Black boxed amino acids from panel A that are known to interact with FAD are located in a6 helix with Asp210 (orange side chain) and His213 (pink side chain) and Lys217 (red side chain) making contacts with the adenine rings