7XGR
Structure of Gemin5 C-terminal region (protomer)
Summary for 7XGR
| Entry DOI | 10.2210/pdb7xgr/pdb |
| Related | 7XDT |
| EMDB information | 33187 |
| 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 | 1 |
| Total formula weight | 75893.88 |
| Authors | |
| 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 Cited by 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: 36056043DOI: 10.1038/s41467-022-32883-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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