Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Visualizing the nucleoplasmic maturation of human pre-60S ribosomal particles.
Journal, issue, pages	Cell Res, Vol. 33, Issue 11, Page 867-878, Year 2023
Publish date	Jul 25, 2023
Authors	Yunyang Zhang / Xiaomeng Liang / Sha Luo / Yan Chen / Yu Li / Chengying Ma / Ningning Li / Ning Gao /
PubMed Abstract	Eukaryotic ribosome assembly is a highly orchestrated process that involves over two hundred protein factors. After early assembly events on nascent rRNA in the nucleolus, pre-60S particles undergo ...Eukaryotic ribosome assembly is a highly orchestrated process that involves over two hundred protein factors. After early assembly events on nascent rRNA in the nucleolus, pre-60S particles undergo continuous maturation steps in the nucleoplasm, and prepare for nuclear export. Here, we report eleven cryo-EM structures of the nuclear pre-60S particles isolated from human cells through epitope-tagged GNL2, at resolutions of 2.8-4.3 Å. These high-resolution snapshots provide fine details for several major structural remodeling events at a virtual temporal resolution. Two new human nuclear factors, L10K and C11orf98, were also identified. Comparative structural analyses reveal that many assembly factors act as successive place holders to control the timing of factor association/dissociation events. They display multi-phasic binding properties for different domains and generate complex binding inter-dependencies as a means to guide the rRNA maturation process towards its mature conformation. Overall, our data reveal that nuclear assembly of human pre-60S particles is generally hierarchical with short branch pathways, and a few factors display specific roles as rRNA chaperones by confining rRNA helices locally to facilitate their folding, such as the C-terminal domain of SDAD1.
External links	Cell Res / PubMed:37491604 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 4.3 Å
Structure data	35370 8idt EMDB-35370, PDB-8idt: human nuclear pre-60S ribosomal particle - State G Method: EM (single particle) / Resolution: 2.8 Å 35371 8idy EMDB-35371, PDB-8idy: human nuclear pre-60S ribosomal particle - State F Method: EM (single particle) / Resolution: 3.0 Å 35375 8ie3 EMDB-35375, PDB-8ie3: human nuclear pre-60S ribosomal particle - State E Method: EM (single particle) / Resolution: 3.3 Å 35596 8ine EMDB-35596, PDB-8ine: human nuclear pre-60S ribosomal particle - State G' Method: EM (single particle) / Resolution: 3.2 Å 35597 8inf EMDB-35597, PDB-8inf: human nuclear pre-60S ribosomal particle - State F' Method: EM (single particle) / Resolution: 3.0 Å 35599 8ink EMDB-35599, PDB-8ink: human nuclear pre-60S ribosomal particle - State D Method: EM (single particle) / Resolution: 3.2 Å 35639 8ipd EMDB-35639, PDB-8ipd: human nuclear pre-60S ribosomal particle - State C Method: EM (single particle) / Resolution: 3.2 Å 35649 8ipx EMDB-35649, PDB-8ipx: human nuclear pre-60S ribosomal particle - State C' Method: EM (single particle) / Resolution: 4.3 Å 35651 8ipy EMDB-35651, PDB-8ipy: human nuclear pre-60S ribosomal particle - State D' Method: EM (single particle) / Resolution: 3.2 Å 35672 8ir1 EMDB-35672, PDB-8ir1: human nuclear pre-60S ribosomal particle - State A Method: EM (single particle) / Resolution: 3.3 Å 35673 8ir3 EMDB-35673, PDB-8ir3: human nuclear pre-60S ribosomal particle - State B' Method: EM (single particle) / Resolution: 3.5 Å
Chemicals	ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-K: Unknown entry ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM
Source	homo sapiens (human)
Keywords	RIBOSOME / GNL2 / nuclear / pre-60S