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TitleCryo-EM structure of human MG53 homodimer.
Journal, issue, pagesBiochem J, Vol. 479, Issue 17, Page 1909-1916, Year 2022
Publish dateSep 16, 2022
AuthorsYange Niu / Gengjia Chen / Fengxiang Lv / Rui-Ping Xiao / Xinli Hu / Lei Chen /
PubMed AbstractMG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a ...MG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a 'body' and two 'wings'. Intermolecular interactions are mainly distributed in the 'body' which is relatively stable, while two 'wings' are more dynamic. The overall architecture of MG53 is distinct from those of TRIM20 and TRIM25, illustrating the broad structural diversity of this protein family.
External linksBiochem J / PubMed:36053137
MethodsEM (single particle)
Resolution3.5 Å
Structure data

33606

7y4s

EMDB-33606, PDB-7y4s:
Structure of human MG53 homo-dimer
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / Tripartite motif-containing protein 72 / MG53 / TRIM72 / Membrane repair / PRY-SPRY domain / Mitsugumin-53

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