Circular assemblies.
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.
Antson
A A
AA
Department of Chemistry, University of York, UK. fred@yorvic.york.ac.uk
Dodson
E J
EJ
Dodson
G G
GG
D001426:Bacterial Proteins; D018834:Chaperonin 60 / Q000737:chemistry; D003546:Cysteine Endopeptidases / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances; D009097:Multienzyme Complexes / Q000737:chemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry; D000683:Serum Amyloid P-Component / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry
D001426:Bacterial Proteins; D018834:Chaperonin 60; D046911:Macromolecular Substances; C079092:MtrB protein, Bacteria; D009097:Multienzyme Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D011506:Proteins; D016601:RNA-Binding Proteins; D000683:Serum Amyloid P-Component; D014157:Transcription Factors; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex