The Functional Differences between the GroEL Chaperonin of <i>Escherichia coli</i> and the HtpB Chaperonin of <i>Legionella pneumophila</i> Can Be Mapped to Specific Amino Acid Residues

The Functional Differences between the GroEL Chaperonin of <i>Escherichia coli</i> and the HtpB Chaperonin of <i>Legionella pneumophila</i> Can Be Mapped to Specific Amino Acid Residues

Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles. GroEL, the chaperonin of <i>Escherichia coli</i>, is the archetype of the family. Protein foldi...

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Bibliographic Details
Main Authors: Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:Biomolecules
Subjects:
chaperonin
GroEL
evolutionary trace
ECM29
yeast-two-hybrid
Legionella
Online Access:https://www.mdpi.com/2218-273X/12/1/59

Internet

https://www.mdpi.com/2218-273X/12/1/59

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