7XDT

Structural basis for Gemin5 decamer-mediated mRNA binding

Summary for 7XDT

• Entry DOI: 10.2210/pdb7xdt/pdb
• EMDB information: 33152
• Descriptor: Gem-associated protein 5 (1 entity in total)
• Functional Keywords: rna binding, tpr repeats, decamer, rna translation, rna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 10
• Total formula weight: 758938.75

Authors

Guo, Q.,Zhao, S.,Zhang, K.,Xu, C. (deposition date: 2022-03-28, release date: 2022-08-24, Last modification date: 2024-06-26)

Primary citation

Guo, Q.,Zhao, S.,Francisco-Velilla, R.,Zhang, J.,Embarc-Buh, A.,Abellan, S.,Lv, M.,Tang, P.,Gong, Q.,Shen, H.,Sun, L.,Yao, X.,Min, J.,Shi, Y.,Martinez-Salas, E.,Zhang, K.,Xu, C.
Structural basis for Gemin5 decamer-mediated mRNA binding.
Nat Commun, 13:5166-5166, 2022

PubMed Abstract: Gemin5 in the Survival Motor Neuron (SMN) complex serves as the RNA-binding protein to deliver small nuclear RNAs (snRNAs) to the small nuclear ribonucleoprotein Sm complex via its N-terminal WD40 domain. Additionally, the C-terminal region plays an important role in regulating RNA translation by directly binding to viral RNAs and cellular mRNAs. Here, we present the three-dimensional structure of the Gemin5 C-terminal region, which adopts a homodecamer architecture comprised of a dimer of pentamers. By structural analysis, mutagenesis, and RNA-binding assays, we find that the intact pentamer/decamer is critical for the Gemin5 C-terminal region to bind cognate RNA ligands and to regulate mRNA translation. The Gemin5 high-order architecture is assembled via pentamerization, allowing binding to RNA ligands in a coordinated manner. We propose a model depicting the regulatory role of Gemin5 in selective RNA binding and translation. Therefore, our work provides insights into the SMN complex-independent function of Gemin5.

PubMed: 36056043
DOI: 10.1038/s41467-022-32883-z

Experimental method

ELECTRON MICROSCOPY (3.31 Å)