Structural and Dynamical Features of Inteins and Implications on Protein Splicing*
+ Author Affiliations
- ↵1 To whom correspondence should be addressed. Tel.: 718-430-8621; E-mail: david.cowburn@einstein.yu.edu.
Abstract
Protein splicing is a posttranslational modification where intervening proteins (inteins) cleave themselves from larger precursor proteins and ligate their flanking polypeptides (exteins) through a multistep chemical reaction. First thought to be an anomaly found in only a few organisms, protein splicing by inteins has since been observed in microorganisms from all domains of life. Despite this broad phylogenetic distribution, all inteins share common structural features such as a horseshoe-like pseudo two-fold symmetric fold, several canonical sequence motifs, and similar splicing mechanisms. Intriguingly, the splicing efficiencies and substrate specificity of different inteins vary considerably, reflecting subtle changes in the chemical mechanism of splicing, linked to their local structure and dynamics. As intein chemistry has widespread use in protein chemistry, understanding the structural and dynamical aspects of inteins is crucial for intein engineering and the improvement of intein-based technologies.
- NMR
- Protein Engineering
- Protein Folding
- Protein Structure
- Protein-Protein Interactions
- Intein
- Protein Splicing
Footnotes
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↵* This work was supported, in whole or in part, by National Institutes of Health Grant GM086868 (to D. C.). This is the third article in the Thematic Minireview Series “Inteins.”
- © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
