Crystal structure of yeast Gid10 in complex with Pro/N-degron

Jin Seok Shin, Si Hoon Park, Leehyeon Kim, Jiwon Heo, Hyun Kyu Song

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


The cellular glucose level has to be tightly regulated by a variety of cellular processes. One of them is the degradation of gluconeogenic enzymes such as Fbp1, Icl1, Mdh2, and Pck1 by GID (glucose-induced degradation deficient) E3 ubiquitin ligase. The Gid4 component of the GID ligase complex is responsible for recognizing the N-terminal proline residue of the target substrates under normal conditions. However, an alternative N-recognin Gid10 controls the degradation process under stressed conditions. Although Gid10 shares a high sequence similarity with Gid4, their substrate specificities are quite different. Here, we report the structure of Gid10 from Saccharomyces cerevisiae in complex with Pro/N-degron, Pro-Tyr-Ile-Thr, which is almost identical to the sequence of the natural substrate Art2. Although Gid10 shares many structural features with the Gid4 protein from yeast and humans, the current structure explains the unique structural difference for the preference of bulky hydrophobic residue at the second position of Pro/N-degron. Therefore, this study provides a fundamental basis for understanding of the structural diversity and substrate specificity of recognition components in the GID E3 ligase complex involved in the Pro/N-degron pathway.

Original languageEnglish
Pages (from-to)86-92
Number of pages7
JournalBiochemical and biophysical research communications
Publication statusPublished - 2021 Dec 10

Bibliographical note

Funding Information:
We thank the staff at beamlines 5C and 11C at the Pohang Accelerator Laboratory, Korea. This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Korean government ( 2021R1A6A3A01088067 to J.S.S.; 2020R1A2C3008285 and 2020R1A5A1019023 to H.K.S.). This work was also partially supported by the Korea University Grant.

Publisher Copyright:
© 2021 Elsevier Inc.


  • E3 ubiquitin ligase
  • GID complex
  • N-degron
  • Proline
  • Saccharomyces cerevisiae
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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