NMR resonance assignments of human Atg3 in aqueous solution and bicelles

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.



Work Title NMR resonance assignments of human Atg3 in aqueous solution and bicelles
Open Access
  1. Yansheng Ye
  2. Guifang Wang
  3. Maria C. Bewley
  4. Hong-Gang Wang
  5. Fang Tian
License In Copyright (Rights Reserved)
Work Type Article
  1. Biomolecular NMR Assignments
Publication Date October 1, 2021
Publisher Identifier (DOI)
  1. https://doi.org/10.1007/s12104-021-10040-9
Deposited November 28, 2021




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Work History

Version 1

  • Created
  • Added Atg3-assignment-revision.pdf
  • Added Creator Yansheng Ye
  • Added Creator Guifang Wang
  • Added Creator Maria C. Bewley
  • Added Creator Hong-Gang Wang
  • Added Creator Fang Tian
  • Published
  • Updated
  • Updated