6elz | pdb_00006elz

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State E (TAP-Flag-Ytm1 E80A) - Visualizing the assembly pathway of nucleolar pre-60S ribosmes

spinqualitylabelsall models 6elz, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6elz is a 54 chain structure with sequence from Saccharomyces cerevisiae, Saccharomyces cerevisiae (strain atcc 204508 / s288c) and Saccharomyces cerevisiae (strain yjm789). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Activity: RNA helicase, with EC number 3.6.4.13 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 [ERB1_YEAST] Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.[HAMAP-Rule:MF_03027] [CIC1_YEAST] An adapter protein that specifically links the 26S proteasome to its substrate CDC4 which is one of the substrate recognition subunits of the SCF E3 ubiquitin ligase complex. Required for turnover of cell cycle regulatory proteins CDC4 and GRR1. Required for synthesis and nuclear export of 60S ribosomal subunits. Required for vegetative growth. [RL37A_YEAST] Binds to the 23S rRNA (By similarity). [NSA2_YEAS7] Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles. Under normal, rapid growth conditions, high levels of NSA2 would allow the progression of pre-60S particles through the ITS2 processing (By similarity). [SPB1_YEAST] Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation.[HAMAP-Rule:MF_03163] [RL25_YEAST] This protein binds to a specific region on the 26S rRNA. [BRX1_YEAST] Required for biogenesis of the 60S ribosomal subunit. [MRT4_YEAST] Involved in mRNA turnover and ribosome assembly. [NOP16_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. [RLP7_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs. [NOP2_YEAST] S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA. Required for 60S ribosomal subunit synthesis and processing. [RL4A_YEAST] Participates in the regulation of the accumulation of its own mRNA. [NOC3_YEAST] Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm. Also required for initiation of DNA replication. May function downstream of the origin recognition complex (ORC complex) in the loading of CDC6 and the minichromosome maintenance complex (MCM complex) onto chromatin during the G1 phase of the cell cycle. Essential for growth. [PESC_YEAS7] Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.[HAMAP-Rule:MF_03028] [NIP7_YEAST] Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly. [EBP2_YEAST] Required for the processing of the 27S pre-rRNA. Probably involved in the step of the processing of the 27 SA precursor into the 27 SB intermediate. [NUG1_YEAST] GTPase required for 60S ribosomal subunit export to the cytoplasm. [RLP24_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of NOG1 to pre-60S particles. [NOP15_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. Required for pre-rRNA processing and cytokinesis. Associates with the precursors of the 25S and 5.8S rRNAs. [HAS1_YEAST] ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. [YTM1_YEAS7] Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.[HAMAP-Rule:MF_03029] [NOG1_YEAST] Involved in the biogenesis of the 60S ribosomal subunit. [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. Publication Abstract from PubMed Eukaryotic 60S ribosomal subunits are comprised of three rRNAs and approximately 50 ribosomal proteins. The initial steps of their formation take place in the nucleolus, but, owing to a lack of structural information, this process is poorly understood. Using cryo-EM, we solved structures of early 60S biogenesis intermediates at 3.3 A to 4.5 A resolution, thereby providing insights into their sequential folding and assembly pathway. Besides revealing distinct immature rRNA conformations, we map 25 assembly factors in six different assembly states. Notably, the Nsa1-Rrp1-Rpf1-Mak16 module stabilizes the solvent side of the 60S subunit, and the Erb1-Ytm1-Nop7 complex organizes and connects through Erb1's meandering N-terminal extension, eight assembly factors, three ribosomal proteins, and three 25S rRNA domains. Our structural snapshots reveal the order of integration and compaction of the six major 60S domains within early nucleolar 60S particles developing stepwise from the solvent side around the exit tunnel to the central protuberance. Visualizing the Assembly Pathway of Nucleolar Pre-60S Ribosomes.,Kater L, Thoms M, Barrio-Garcia C, Cheng J, Ismail S, Ahmed YL, Bange G, Kressler D, Berninghausen O, Sinning I, Hurt E, Beckmann R Cell. 2017 Dec 14;171(7):1599-1610.e14. doi: 10.1016/j.cell.2017.11.039. PMID:29245012 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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