TY - JOUR
T1 - NMR resonance assignments of human Atg3 in aqueous solution and bicelles
AU - Ye, Yansheng
AU - Wang, Guifang
AU - Bewley, Maria C.
AU - Wang, Hong Gang
AU - Tian, Fang
N1 - Funding Information:
We gratefully acknowledge Dr. Xuejun Jiang’s lab for providing the expression vector. We are thankful for financial support from the National Institutes of Health NIGMS (1R01GM127730 and 1R01GM127954) and the Four Diamonds Fund.
Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Nature B.V.
PY - 2021/10
Y1 - 2021/10
N2 - 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.
AB - 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.
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U2 - 10.1007/s12104-021-10040-9
DO - 10.1007/s12104-021-10040-9
M3 - Article
C2 - 34296398
AN - SCOPUS:85112197725
SN - 1874-2718
VL - 15
SP - 421
EP - 425
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 2
ER -