Correct Folding of Circularly Permuted Variants of a βα Barrel Enzyme in vivo

An important question in protein folding is whether the natural amino and carboxyl termini and the given order of secondary structure segments are critical to the stability and to the folding pathway of proteins. Here it is shown that two circularly permuted versions of the gene of a single-domain β...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1989-01, Vol.243 (4888), p.206-210
Main Authors: Luger, Karolin, Hommel, Ulrich, Herold, Marzell, Hofsteenge, Jan, Kirschner, Kasper
Format: Article
Language:English
Subjects:
Active sites
Amino acids
Biological and medical sciences
Enzymes
Fluorescence
Fundamental and applied biological sciences. Psychology
Gels
Genetic vectors
Molecular biophysics
Plasmids
Protein folding
Protein refolding
Proteins
Structure in molecular biology
Tridimensional structure
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Summary:An important question in protein folding is whether the natural amino and carboxyl termini and the given order of secondary structure segments are critical to the stability and to the folding pathway of proteins. Here it is shown that two circularly permuted versions of the gene of a single-domain βα barrel enzyme can be expressed in Escherichia coli. The variants are enzymically active and are practically indistinguishable from the original enzyme by several structural and spectroscopic criteria, despite the creation of new termini and the cleavage of a surface loop. This novel genetic approach should be useful for protein folding studies both in vitro and in vivo.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2643160