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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Structural and Functional Diversity of Nudix Fold

Author(s): Yuejin Hua, Jun Lin and Bing Tian

Volume 15 , Issue 1 , 2008

Page: [108 - 112] Pages: 5

DOI: 10.2174/092986608783330350

Price: $65

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.

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


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