What's the Key to Unlocking the Proteasome's Gate?

Andres H de la Peña; Gabriel C Lander

doi:10.1016/j.str.2016.11.011

What's the Key to Unlocking the Proteasome's Gate?

Structure. 2016 Dec 6;24(12):2037-2038. doi: 10.1016/j.str.2016.11.011.

Authors

Andres H de la Peña¹, Gabriel C Lander²

Affiliations

¹ Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA.
² 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.

PMID: 27926830
DOI: 10.1016/j.str.2016.11.011

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.

Publication types

Comment

MeSH terms

Proteasome Endopeptidase Complex / chemistry*

Substances

Proteasome Endopeptidase Complex