Cryo-EM structure of human MG53 homodimer

Yange Niu; Gengjia Chen; Fengxiang Lv; Rui-Ping Xiao; Xinli Hu; Lei Chen

doi:10.1042/BCJ20220385

Cryo-EM structure of human MG53 homodimer

Biochem J. 2022 Sep 16;479(17):1909-1916. doi: 10.1042/BCJ20220385.

Authors

Yange Niu^#^{1

2}, Gengjia Chen^#^{1

2}, Fengxiang Lv¹, Rui-Ping Xiao^{1

3}, Xinli Hu¹, Lei Chen^{1

2

3}

Affiliations

¹ State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing 100871, China.
² National Biomedical Imaging Center, Peking University, Beijing 100871, China.
³ Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China.

^# Contributed equally.

PMID: 36053137
DOI: 10.1042/BCJ20220385

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 '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.

Keywords: E3 ligase; MG53; TRIM; TRIM72.

MeSH terms

Carrier Proteins* / metabolism
Cryoelectron Microscopy
Humans
Membrane Proteins* / metabolism
Protein Multimerization
Tripartite Motif Proteins / chemistry*
Tripartite Motif Proteins / metabolism
Ubiquitin-Protein Ligases / metabolism

Substances

Carrier Proteins
Membrane Proteins
TRIM72 protein, human
Tripartite Motif Proteins
Ubiquitin-Protein Ligases