title: Structural and functional diversity of Nudix fold.
abstract: Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates linked to other moieties X, and contain the sequence motif or Nudix box, GX5EX7REUXEEXGU. The mechanisms of Nudix hydrolases are highly diverse in the position on the substrate. In this paper, we examined the sequences and structures of the MutT/Nudix superfamily. And two recent developed methods were employed for data analyses of the superfamily. One is QH method evaluating the similarities among structures for structural phylogeny. The other method is clustering analysis by using the CLANS program that could analysis thousands of sequences of the full dataset rather than the representative sequences of the superfamily. Finally, we proposed a more objective classification of the MutT/Nudix superfamily members based on detailed sequence and structure analyses.
authors.affiliation: Institute of Nuclear-Agricultural Sciences, Key Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Zhejiang University, 310029, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Lin
authors.forename: Bing
authors.initials: B
authors.lastname: Tian
authors.forename: Yuejin
authors.initials: Y
authors.lastname: Hua
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D016000:Cluster Analysis; D010802:Phylogeny; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011755:Pyrophosphatases / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment; D000096964:Nudix Hydrolases
chemical_list: D011755:Pyrophosphatases; D000096964:Nudix Hydrolases