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• W2029542234 endingPage "4105" @default.
• W2029542234 startingPage "4098" @default.
• W2029542234 abstract "Proteasome-dependent proteolysis is essential for a number of key cellular processes and requires a sophisticated biogenesis pathway to function. Here, we have arrested the assembly process in its dynamic progression at the short-lived 16S state. Structural analysis of the 16S proteasome precursor intermediates by electron microscopy, and single particle analysis reveals major conformational changes in the structure of the β-ring in comparison with one-half of the 20S proteasome. The individual β-subunits in the 16S precursor complex rotate with respect to their positions in the x-ray crystallographic structure of the fully assembled 20S. This rearrangement results in a movement of the catalytic residue threonine-1 from the protected location in 16S precursor complexes to a more exposed position in the 20S structure. Thereby, our findings provide a molecular explanation for the structural rearrangements necessary for the dimerization of two 16S precursor complexes and the subsequent final maturation to active 20S proteasomes." @default.
• W2029542234 created "2016-06-24" @default.
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• W2029542234 date "2004-12-01" @default.
• W2029542234 modified "2023-09-30" @default.
• W2029542234 title "Rearrangement of the 16S Precursor Subunits Is Essential for the Formation of the Active 20S Proteasome" @default.
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• W2029542234 doi "https://doi.org/10.1529/biophysj.104.051144" @default.
• W2029542234 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1304918" @default.
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• W2029542234 hasPublicationYear "2004" @default.
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