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

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

Author information

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.

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.

PMID:
27926830
DOI:
10.1016/j.str.2016.11.011
[Indexed for MEDLINE]
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