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Structure of 20S proteasome from yeast at 2.4Å resolution
Two β-type subunits are processed to an intermediate form, indicating that an additional nonspecific endopeptidase activity may exist which is important for peptide hydrolysis and for the generation of ligands for class I molecules of the major histocompatibility complex.
A gated channel into the proteasome core particle
Crystallographic analysis showed that deletion of the tail of the α3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis.
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the HSp90 chaperone system in eukaryotes and it is shown that TPR2A is the high affinity Hsp90‐binding site and TPR1 and T PR2B bind HSP70 with moderate affinity.
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
It is reported that Rpn13, a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 to the proteasomes, and a novel ubiquitIn-binding mode in which loops rather than secondary structural elements are used to capture ubiqu itin.
Probing the reaction mechanism of IspH protein by x-ray structure analysis
The five crystal structures of IspH in complex with substrate, converted substrate, products and PPi reported in this article provide unique insights into the mechanism of this enzyme.