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Structural and Functional Diversity of Nudix Fold

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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.

Keywords: DNA repair; MutT/Nudix superfamily; QH; RMSD; cluster analysis; structural phylogeny

Document Type: Research Article


Publication date: 2008-01-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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