Circular assemblies

Curr Opin Struct Biol. 1996 Apr;6(2):142-50. doi: 10.1016/s0959-440x(96)80067-4.

Abstract

During 1994 and 1995, the structures of the serum amyloid P component, the bacterial chaperonin GroEL, the 20S proteasome, the bacterial light-harvesting complexes and the tryptophan operon RNA-binding attenuation protein have been determined. These structures all form circular assemblies in which the individual subunits are related by rotational symmetry. In most cases the circular organization generates a new biophysical property and a specific biological function which have presumably been selected by evolution.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins*
  • Chaperonin 60 / chemistry
  • Cysteine Endopeptidases / chemistry
  • Humans
  • Macromolecular Substances
  • Multienzyme Complexes / chemistry
  • Photosynthetic Reaction Center Complex Proteins / chemistry
  • Proteasome Endopeptidase Complex
  • Protein Conformation*
  • Protein Folding
  • Proteins / chemistry*
  • RNA-Binding Proteins / chemistry
  • Serum Amyloid P-Component / chemistry
  • Transcription Factors / chemistry

Substances

  • Bacterial Proteins
  • Chaperonin 60
  • Macromolecular Substances
  • MtrB protein, Bacteria
  • Multienzyme Complexes
  • Photosynthetic Reaction Center Complex Proteins
  • Proteins
  • RNA-Binding Proteins
  • Serum Amyloid P-Component
  • Transcription Factors
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex