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
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Bacterial Proteins*
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Chaperonin 60 / chemistry
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Cysteine Endopeptidases / chemistry
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Humans
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Macromolecular Substances
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Multienzyme Complexes / chemistry
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Photosynthetic Reaction Center Complex Proteins / chemistry
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Proteasome Endopeptidase Complex
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Protein Conformation*
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Protein Folding
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Proteins / chemistry*
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RNA-Binding Proteins / chemistry
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Serum Amyloid P-Component / chemistry
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Transcription Factors / chemistry
Substances
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Bacterial Proteins
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Chaperonin 60
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Macromolecular Substances
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MtrB protein, Bacteria
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Multienzyme Complexes
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Photosynthetic Reaction Center Complex Proteins
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Proteins
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RNA-Binding Proteins
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Serum Amyloid P-Component
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Transcription Factors
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex