@article{715d3b1df76b489187b7e07c2238b9b5,
title = "A gated channel into the proteasome core particle",
abstract = "The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (α) ring subunits. 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. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the α-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.",
author = "Michael Groll and Monica Bajorek and Alwin K{\"o}hler and Luis Moroder and Rubin, {David M.} and Robert Huber and Glickman, {Michael H.} and Daniel Finley",
note = "Funding Information: This work was supported by the NIH grant (to D.F.), the Foundation for the Promotion of Research at the Technion (M.H.G.), The US-Israel Binational Science Foundation (to M.H.G. and D.F.) and the Deutsche Forschungsgemeinschaft (to R.H.). A.K. was partially supported by a fellowship from the Studienfoerderung Cusanuswerk. The authors thank C. Larsen and G. Dittmar (Harvard) for generous assistance with computer imaging, K. Mann (Max-Planck-Institut f{\"u}r Biochemie, Martinsried, Germany) for help with N-terminal sequence analysis, and G. Bourenkow and H. Bartunik (DESY, Hamburg, Germany) for assistance with X-ray experiments.",
year = "2000",
doi = "10.1038/80992",
language = "English",
volume = "7",
pages = "1062--1067",
journal = "Nature Structural Biology",
issn = "1072-8368",
publisher = "Nature Publishing Group",
number = "11",
}