title: What's the Key to Unlocking the Proteasome's Gate?
abstract: In this issue of Structure, Bolten et al. (2016) describe the organization of the mycobacterial proteasome in complex with the ATP-independent bacterial proteasome activator (Bpa, PafE). They confirm several activation motifs employed by archaea and eukaryotes and highlight differences that pose Bpa as a novel architectural class of proteasome activators.
authors.affiliation: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA.
authors.forename: Andres H
authors.initials: AH
authors.lastname: de la Peña
authors.affiliation: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA. Electronic address: glander@scripps.edu.
authors.forename: Gabriel C
authors.initials: GC
authors.lastname: Lander
mesh_terms: D046988:Proteasome Endopeptidase Complex / Q000737:chemistry*
chemical_list: D046988:Proteasome Endopeptidase Complex