9hny

Mitoribosomal small subunit in complex with Mettl15 and Mettl17

spinqualitylabelsall models 9hny, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hny is a 10 chain structure with sequence from Trypanosoma brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: ACO, GTP, MG, PO4, SAM, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A3L6L8G2_9TRYP Publication Abstract from PubMed The assembly of the mitoribosomal small subunit involves folding and modification of rRNA, and its association with mitoribosomal proteins. This process is assisted by a dynamic network of assembly factors. Conserved methyltransferases Mettl15 and Mettl17 act on the solvent-exposed surface of rRNA. Binding of Mettl17 is associated with the early assembly stage, whereas Mettl15 is involved in the late stage, but the mechanism of transition between the two was unclear. Here, we integrate structural data from Trypanosoma brucei with mammalian homologs and molecular dynamics simulations. We reveal how the interplay of Mettl15 and Mettl17 in intermediate steps links the distinct stages of small subunit assembly. The analysis suggests a model wherein Mettl17 acts as a platform for Mettl15 recruitment. Subsequent release of Mettl17 allows a conformational change of Mettl15 for substrate recognition. Upon methylation, Mettl15 adopts a loosely bound state which ultimately leads to its replacement by initiation factors, concluding the assembly. Together, our results indicate that assembly factors Mettl15 and Mettl17 cooperate to regulate the biogenesis process, and present a structural data resource for understanding molecular adaptations of assembly factors in mitoribosome. Mettl15-Mettl17 modulates the transition from early to late pre-mitoribosome.,Zgadzay Y, Mirabello C, Wanes G, Panek T, Chauhan P, Nystedt B, Zikova A, Whitford PC, Gahura O, Amunts A bioRxiv [Preprint]. 2025 Jan 24:2024.12.18.629302. doi: , 10.1101/2024.12.18.629302. PMID:39896671 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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