9r3a

Structure of Stalled Beta-Galactosidase 70S Ribosome Nascent Chain

spinqualitylabelsall models 9r3a, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9r3a is a 10 chain structure with sequence from Escherichia coli and Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.86Å Ligands: 1MG, 2MA, 2MG, 3TD, 4D4, 5MC, 5MU, 6MZ, G7M, H2U, IAS, K, MA6, MG, MS6, OMC, OMG, OMU, PRO, PSU, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL35_ECOLI Publication Abstract from PubMed Natural proteins often form intricate multidomain, oligomeric architectures. This presents a prima facie challenge to cellular homeostasis, as topologically complex proteins seldom refold efficiently in vitro. Here, we show that the efficient folding and assembly of the five-domain homotetramer beta-galactosidase is obligatorily coupled to its synthesis on the ribosome, and we define the underlying mechanisms. During refolding from a denaturant, maturation of the catalytic domain is frustrated. Assembly outpaces monomer folding, and non-native oligomers accumulate. Efficient de novo folding is characterized by segmental domain folding, shaped by the binding of a nascent amphipathic helix to a cryptic pocket on uL23 on the ribosome surface. Homomer assembly also initiates cotranslationally via recruitment of a full-length subunit to the nascent polypeptide, and the failure to do so results in misassembly. Our results reveal how the ribosome can dictate the timing of folding and assembly to enable efficient biogenesis of a topologically complex protein. The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis.,Roeselova A, Shivakumaraswamy S, Jurkeviciute G, He JZ, Auburger J, Schmitt JL, Kramer G, Bukau B, Enchev RI, Balchin D Mol Cell. 2026 Jan 19:S1097-2765(25)01021-4. doi: 10.1016/j.molcel.2025.12.022. PMID:41558483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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