NMR resonance assignments of human Atg3 in aqueous solution and bicelles

Yansheng Ye, Guifang Wang, Maria C. Bewley, Hong Gang Wang, Fang Tian

Research output: Contribution to journalArticlepeer-review

Abstract

Human Atg3 (hAtg3) is an E2-like enzyme that catalyzes the conjugation of LC3 family proteins to phosphatidylethanolamine (PE) lipids in the autophagosomal membrane during autophagy. The reaction product, LC3-PE, acts as a marker for autophagic cargo and is required for the effective construction of functional autophagosomes. However, the structural and molecular basis of this conjugation reaction remains elusive, at least in part, because of the absence of lipid bilayers in structural studies conducted to date. Here, we report a sequential resonance assignment for an hAtg3 construct both in aqueous solution and in bicelles. hAtg3 has 314 residues, and our construct lacks the unstructured region from residues 90 to 190. Our results demonstrate a structural rearrangement of hAtg3 N-terminus when it interacts with membranes.

Original languageEnglish (US)
Pages (from-to)421-425
Number of pages5
JournalBiomolecular NMR Assignments
Volume15
Issue number2
DOIs
StatePublished - Oct 2021

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

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