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Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: Jun 1, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Structural changes underlying allostery in group II chaperonins.

Keith R Willison¹

¹Section of Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London SW36JB, UK. keith.willison@icr.ac.uk

Structure (London, England : 1993)

|June 8, 2011

Summary

The chaperonin from Methanococcus maripaludis requires ATP hydrolysis, not just binding, for its folding chamber to fully close. This finding is crucial for understanding protein folding mechanisms in archaea.

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Area of Science:

Biochemistry
Structural Biology
Microbiology

Background:

The chaperonin from Methanococcus maripaludis (Mm-cpn) is a 16-subunit homo-oligomeric protein complex involved in protein folding.
Understanding the mechanism of chaperonin function, particularly the role of ATP, is essential for cellular protein homeostasis.

Discussion:

Single particle cryo-electron microscopy was used to investigate the ATP-dependence of folding chamber closure in Mm-cpn.
The study observed that ATP binding alone induces a partial rotation and slight closure of the chaperonin's cavity.
Complete closure of the folding chamber is contingent upon ATP hydrolysis, indicating a multi-step process.

Key Insights:

ATP binding initiates conformational changes in Mm-cpn, including a ~45° rigid body rotation.
ATP hydrolysis is the critical step driving the full closure of the chaperonin's central cavity.
The mechanism highlights the distinct roles of ATP binding versus hydrolysis in chaperonin-mediated protein folding.

Outlook:

Further research can explore the structural dynamics of Mm-cpn during the entire ATP hydrolysis cycle.
Investigating other archaeal chaperonins may reveal conserved or divergent mechanisms of ATP-dependent conformational changes.
This work provides a foundation for understanding how chaperonins facilitate protein folding in extreme environments.