7EL6

Structure of SMCR8 bound FEM1B

Summary for 7EL6

• Entry DOI: 10.2210/pdb7el6/pdb
• Descriptor: Protein fem-1 homolog B,Guanine nucleotide exchange protein SMCR8 (1 entity in total)
• Functional Keywords: ubiquitination e3 ligase, peptide binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 78603.55

Authors

Zhao, S.,Xu, C. (deposition date: 2021-04-08, release date: 2021-05-12, Last modification date: 2023-11-29)

Primary citation

Zhao, S.,Ru, W.,Chen, X.,Liao, S.,Zhu, Z.,Zhang, J.,Xu, C.
Structural insights into SMCR8 C-degron recognition by FEM1B.
Biochem.Biophys.Res.Commun., 557:236-239, 2021

PubMed Abstract: C-degrons play critical roles in targeting the receptor proteins of Cullin-RING E3 ligase complexes to initiate protein degradation. FEM1 proteins, including FEM1A, FEM1B, and FEM1C, act as the receptors to specifically recognize Arg/C-degrons to enable CRL2-mediated protein turnover. Very few substrates have been identified for FEM1B, except CDK5R1. We found that CRL2 also recognizes the C-degron of an SMCR8 isoform, and uncovered the recognition of SMCR8 by FEM1B through presenting the structure of FEM1B bound to SMCR8. Our work provides insights into the role of CRL2 in regulating the lifetime of SMCR8, a critical autophagy regulator.

PubMed: 33892462
DOI: 10.1016/j.bbrc.2021.04.046

Experimental method

X-RAY DIFFRACTION (2.802 Å)