6t59 | pdb_00006t59

Structure of rabbit 80S ribosome translating beta-tubulin in complex with tetratricopeptide protein 5 and nascent chain-associated complex

spinqualitylabelsall models 6t59, resolution 3.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t59 is a 53 chain structure with sequence from [1] and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, ZN NonStd Res: UNK Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [U3KPD5_RABIT] Binds to the 23S rRNA.[RuleBase:RU000576] [TTC5_HUMAN] Adapter protein involved in p53/TP53 response that acts by regulating and mediating the assembly of multi-protein complexes. Required to facilitate the interaction between JMY and p300/EP300 and increase p53/TP53-dependent transcription and apoptosis. Prevents p53/TP53 degradation by MDM2 (By similarity). Publication Abstract from PubMed Tubulins play crucial roles in cell division, intracellular traffic, and cell shape. Tubulin concentration is autoregulated by feedback control of mRNA degradation via an unknown mechanism. Here, we identified tetratricopeptide protein 5 (TTC5) as a tubulin-specific ribosome-associating factor that triggers co-translational degradation of tubulin mRNAs in response to excess soluble tubulin. Structural analysis revealed that TTC5 binds near the ribosome exit tunnel and engages the N terminus of nascent tubulins. TTC5 mutants incapable of ribosome or nascent tubulin interaction abolished tubulin autoregulation and showed chromosome segregation defects during mitosis. Our findings show how a subset of mRNAs can be targeted for coordinated degradation by a specificity factor that recognizes the nascent polypeptides they encode. TTC5 mediates autoregulation of tubulin via mRNA degradation.,Lin Z, Gasic I, Chandrasekaran V, Peters N, Shao S, Mitchison TJ, Hegde RS Science. 2019 Nov 14. pii: science.aaz4352. doi: 10.1126/science.aaz4352. PMID:31727855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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