ausblenden:
Schlagwörter:
Proteasome; Multicatalytic proteinase; Pa28 activator; Thermoplasma acidophilum; Electron microscopy.; Protein secondary structure; Tat-mediated transactivation; Molecular-weight proteases; Rabbit reticulocyte lysate; Thermoplasma-acidophilum; Escherichia-coli; Crystal-structure; 3-dimensional structure; Structure prediction.; Experimental biology & medicine.
Zusammenfassung:
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation and has a highly conserved structure from slime molds to humans. The elongated molecule which has a molecular mass of approximately 2,000 kD is formed by a barrel-shaped 20S core complex and two polar 19S complexes. The 20S complex has C2 symmetry and is built by four seven-membered rings of which the outer rings are rotated by 26 degrees relative to the inner rings while the inner rings are in register. The 19S cap complex is asymmetric and therefore considerably less well understood on a structural level. From a comparison of the activity and regulation of the 26S and 20S particles, it can be deduced that the 20S particle contains the protease activity while the 19S complex is supposed to contain isopeptidase, oxidoreductase, ATPase and protein-unfolding activities. In this article we describe the structure of various proteasome complexes as determined by electron microscopy and discuss structural implications of their subunit sequences. [References: 73]
