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-Structure paper
Title | Cryo-EM structure of human MG53 homodimer. |
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Journal, issue, pages | Biochem J, Vol. 479, Issue 17, Page 1909-1916, Year 2022 |
Publish date | Sep 16, 2022 |
Authors | Yange Niu / Gengjia Chen / Fengxiang Lv / Rui-Ping Xiao / Xinli Hu / Lei Chen / |
PubMed Abstract | 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 ...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 links | Biochem J / PubMed:36053137 |
Methods | EM (single particle) |
Resolution | 3.5 Å |
Structure data | EMDB-33606, PDB-7y4s: |
Source |
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Keywords | STRUCTURAL PROTEIN / Tripartite motif-containing protein 72 / MG53 / TRIM72 / Membrane repair / PRY-SPRY domain / Mitsugumin-53 |