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Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

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Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

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Protein Organization01:13

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Metamorphic proteins mediate evolutionary transitions of structure.

Itamar Yadid1, Noam Kirshenbaum, Michal Sharon

  • 1Department of Biological Chemistry, and Israel Structural Proteomics Center, Weizmann Institute of Science, Rehovot 76100, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|April 7, 2010
PubMed
Summary

Certain proteins can change shape, aiding the evolution of new structures. Researchers evolved new proteins from fragments of tachylectin-2, revealing metamorphic intermediates that facilitate the evolution of beta-propeller protein folds.

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Area of Science:

  • Protein structure and evolution
  • Biochemistry
  • Molecular biology

Background:

  • Protein primary sequence typically dictates a single tertiary and quaternary structure.
  • Metamorphic proteins, capable of reversible backbone rearrangements, offer insights into protein fold evolution.
  • The role of metamorphic intermediates in early protein structure evolution remains under-explored.

Purpose of the Study:

  • To investigate the potential role of metamorphic intermediates in mediating evolutionary transitions of protein structure.
  • To evolve new proteins based on fragments of tachylectin-2 to explore metamorphic properties.
  • To understand how modular and metamorphic protein subunits contribute to structural diversity.

Main Methods:

  • Evolution of new proteins using approximately 100 amino acid fragments from tachylectin-2.
  • Structural analysis of the evolved proteins to determine tertiary and quaternary structures.
  • Investigation of subunit rearrangements, including domain swaps and strand exchanges.

Main Results:

  • Novel beta-propeller structures and unique pentameric assemblies were revealed.
  • Identical protein sequences adopted multiple distinct structures within the oligomeric assembly.
  • Bridging subunits exhibited domain swaps and strand exchanges, enabling the formation of connected propellers.
  • Lectin function was maintained despite significant structural changes.

Conclusions:

  • The modular and metamorphic nature of protein subunits facilitates dramatic changes in structure while preserving function.
  • Evolved oligomers represent putative intermediates for beta-propeller evolution from smaller protein elements.
  • The capacity for a single sequence to adopt multiple structures can be evolutionarily optimized, promoting the emergence of new protein architectures.