5fl8 | pdb_00005fl8

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CRYO-EM STRUCTURE OF THE RIX1-REA1 PRE-60S PARTICLE

spinqualitylabelsall models 5fl8, resolution 9.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fl8 is a 48 chain structure with sequence from Saccharomyces cerevisiae, Saccharomyces cerevisiae and Saccharomyces cerevisiae (strain atcc 204508 / s288c). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [RLP24_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of NOG1 to pre-60S particles. [RL11A_YEAST] Binds to 5S ribosomal RNA. [RL12A_YEAST] This protein binds directly to 26S ribosomal RNA.[HAMAP-Rule:MF_00736] [SDA1_YEAST] Required for 60S pre-ribosomal subunits export to the cytoplasm. May also be required for 60S ribosomal subunit maturation and accumulation. Involved in G1 events and passage through start, and possibly actin cytoskeleton organization. [RL25_YEAST] This protein binds to a specific region on the 26S rRNA. [NOG1_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. [RL4A_YEAST] Participates in the regulation of the accumulation of its own mRNA. [NLE1_YEAST] Involved in processing and efficient intra-nuclear transport or pre-60S ribosomal subunits. Forms a complex with REA1 which is essential for ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle. [MRT4_YEAST] Involved in mRNA turnover and ribosome assembly. [RL5_YEAST] Binds 5S RNA and is required for 60S subunit assembly. [RL37A_YEAST] Binds to the 23S rRNA (By similarity). [IF6_YEAST] Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1. Also required for pre-rRNA processing. [MDN1_YEAST] Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the nucleus. Mediates ATP-dependent remodeling of the pre-ribosome just prior to export to allow maturation of 60S subunits into export-competent particles. Removes the ribosome biogenesis factor RSA4 from pre-60S ribosomal subunits in the nucleoplasm to drive nuclear export of the subunit. Involved in 3' processing of the 5.8S rRNA. Publication Abstract from PubMed Ribosome synthesis is catalyzed by approximately 200 assembly factors, which facilitate efficient production of mature ribosomes. Here, we determined the cryo-EM structure of a Saccharomyces cerevisiae nucleoplasmic pre-60S particle containing the dynein-related 550-kDa Rea1 AAA(+) ATPase and the Rix1 subcomplex. This particle differs from its preceding state, the early Arx1 particle, by two massive structural rearrangements: an approximately 180 degrees rotation of the 5S ribonucleoprotein complex and the central protuberance (CP) rRNA helices, and the removal of the 'foot' structure from the 3' end of the 5.8S rRNA. Progression from the Arx1 to the Rix1 particle was blocked by mutational perturbation of the Rix1-Rea1 interaction but not by a dominant-lethal Rea1 AAA(+) ATPase-ring mutant. After remodeling, the Rix1 subcomplex and Rea1 become suitably positioned to sense correct structural maturation of the CP, which allows unidirectional progression toward mature ribosomes. Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling.,Barrio-Garcia C, Thoms M, Flemming D, Kater L, Berninghausen O, Bassler J, Beckmann R, Hurt E Nat Struct Mol Biol. 2016 Jan;23(1):37-44. doi: 10.1038/nsmb.3132. Epub 2015 Nov , 30. PMID:26619264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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