Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst—A Structural and Functional Analysis

Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst—A Structural and Functional Analysis

Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low, but it could be increased by inserting the chapero...

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Bibliographic Details
Main Authors: Gabriel Žoldák, Thomas A. Knappe, Anne-Juliane Geitner, Christian Scholz, Holger Dobbek, Franz X. Schmid, Roman P. Jakob
Format: Article
Language:English
Published: MDPI AG 2024-03-01
Series:Molecules
Subjects:
protein folding
chaperone
prolyl isomerase
immunophilin
SlyD
SlpA
Online Access:https://www.mdpi.com/1420-3049/29/7/1440

Internet

https://www.mdpi.com/1420-3049/29/7/1440

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