Small but versatile: the extraordinary functional and structural diversity of the β-grasp fold |
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Authors: | A Maxwell Burroughs S Balaji Lakshminarayan M Iyer L Aravind |
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Institution: | (1) National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA;(2) Bioinformatics Program, Boston University, Boston, MA 02215, USA |
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Abstract: | Background The β-grasp fold (β-GF), prototyped by ubiquitin (UB), has been recruited for a strikingly diverse range of biochemical functions.
These functions include providing a scaffold for different enzymatic active sites (e.g. NUDIX phosphohydrolases) and iron-sulfur
clusters, RNA-soluble-ligand and co-factor-binding, sulfur transfer, adaptor functions in signaling, assembly of macromolecular
complexes and post-translational protein modification. To understand the basis for the functional versatility of this small
fold we undertook a comprehensive sequence-structure analysis of the fold and developed a natural classification for its members. |
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