Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA

Volume: 453, Issue: 3, Pages: 493 - 497
Published: Oct 1, 2014
Abstract
Formation of the eukaryotic proteasome is not a spontaneous process but a highly ordered process assisted by several assembly chaperones. In contrast, archaeal proteasome subunits can spontaneously assemble into an active form. Recent bioinformatic analysis identified the proteasome-assembly chaperone-like proteins, PbaA and PbaB, in archaea. Our previous study showed that the PbaB homotetramer functions as a proteasome activator through its...
Paper Details
Title
Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA
Published Date
Oct 1, 2014
Volume
453
Issue
3
Pages
493 - 497
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