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J Biol Chem. 2014 May 23;289(21):14506-11. doi: 10.1074/jbc.R113.540302. Epub 2014 Apr 2.

Structural and dynamical features of inteins and implications on protein splicing.

Author information

1
From the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461 and.
2
the Department of Chemistry, Frick Laboratory, Princeton University, Princeton, New Jersey 08544.
3
From the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461 and 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.

KEYWORDS:

Intein; NMR; Protein Engineering; Protein Folding; Protein Splicing; Protein Structure; Protein-Protein Interactions

PMID:
24695731
PMCID:
PMC4031508
DOI:
10.1074/jbc.R113.540302
[Indexed for MEDLINE]
Free PMC Article

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