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TitleStructural Basis for the Enzymatic Activity of the HACE1 HECT-Type E3 Ligase Through N-Terminal Helix Dimerization.
Journal, issue, pagesAdv Sci (Weinh), Vol. 10, Issue 27, Page e2207672, Year 2023
Publish dateAug 3, 2023
AuthorsSunil Singh / Satoru Machida / Nikhil Kumar Tulsian / Yeu Khai Choong / Joel Ng / Srihari Shankar / Yaochen Liu / Krisha Vashdev Chandiramani / Jian Shi / J Sivaraman /
PubMed AbstractHACE1 is an ankyrin repeat (AKR) containing HECT-type E3 ubiquitin ligase that interacts with and ubiquitinates multiple substrates. While HACE1 is a well-known tumor suppressor, its structure and ...HACE1 is an ankyrin repeat (AKR) containing HECT-type E3 ubiquitin ligase that interacts with and ubiquitinates multiple substrates. While HACE1 is a well-known tumor suppressor, its structure and mode of ubiquitination are not understood. The authors present the cryo-EM structures of human HACE1 along with in vitro functional studies that provide insights into how the enzymatic activity of HACE1 is regulated. HACE1 comprises of an N-terminal AKR domain, a middle (MID) domain, and a C-terminal HECT domain. Its unique G-shaped architecture interacts as a homodimer, with monomers arranged in an antiparallel manner. In this dimeric arrangement, HACE1 ubiquitination activity is hampered, as the N-terminal helix of one monomer restricts access to the C-terminal domain of the other. The in vitro ubiquitination assays, hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis, mutagenesis, and in silico modeling suggest that the HACE1 MID domain plays a crucial role along with the AKRs in RAC1 substrate recognition.
External linksAdv Sci (Weinh) / PubMed:37537642 / PubMed Central
MethodsEM (single particle)
Resolution3.92 - 4.55 Å
Structure data

34551

8h8x

EMDB-34551, PDB-8h8x:
Cryo-EM structure of HACE1 monomer
Method: EM (single particle) / Resolution: 3.92 Å

34586

8hae

EMDB-34586, PDB-8hae:
Cryo-EM structure of HACE1 dimer
Method: EM (single particle) / Resolution: 4.55 Å

Source
  • homo sapiens (human)
KeywordsANTITUMOR PROTEIN / E3 ubiquitin ligase / tumor suppressor / Post-translational modifier / Protein degradation

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