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Single-particle cryoEM data of yeast Ubr1-Ubc2-Ub-Ub-N-degron complex (elongation)

ABSTRACT:

SUBMITTER: Minglei Zhao

PROVIDER: EMPIAR-10902 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural insights into Ubr1-mediated N-degron polyubiquitination.

Pan Man M Zheng Qingyun Q Wang Tian T Liang Lujun L Mao Junxiong J Zuo Chong C Ding Ruichao R Ai Huasong H Xie Yuan Y Si Dong D Yu Yuanyuan Y Liu Lei L Zhao Minglei M

Nature 20211117 7888

The N-degron pathway targets proteins that bear a destabilizing residue at the N terminus for proteasome-dependent degradation<sup>1</sup>. In yeast, Ubr1-a single-subunit E3 ligase-is responsible for the Arg/N-degron pathway<sup>2</sup>. How Ubr1 mediates the initiation of ubiquitination and the elongation of the ubiquitin chain in a linkage-specific manner through a single E2 ubiquitin-conjugating enzyme (Ubc2) remains unknown. Here we developed chemical strategies to mimic the reaction interm ...[more]

PMID: 34789879

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