8ir3: Difference between revisions

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'''Unreleased structure'''


The entry 8ir3 is ON HOLD
==human nuclear pre-60S ribosomal particle - State B'==
<StructureSection load='8ir3' size='340' side='right'caption='[[8ir3]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ir3]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IR3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2MG:2N-METHYLGUANOSINE-5-MONOPHOSPHATE'>2MG</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=A2M:2-O-METHYLADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>A2M</scene>, <scene name='pdbligand=B8K:7-acetyl,+guanosine-5-monophosphate'>B8K</scene>, <scene name='pdbligand=B8Q:3-methyl,+cytidine-5-monophosphate'>B8Q</scene>, <scene name='pdbligand=B8T:4-methyl,+cytidine-5-monophosphate'>B8T</scene>, <scene name='pdbligand=B8W:6-methyl,+guanosine-5-monophosphate'>B8W</scene>, <scene name='pdbligand=B9B:6-propyl,+guanosine-5-monophosphate'>B9B</scene>, <scene name='pdbligand=B9H:2-methyl,+3-propyl,+cytidine-5-monophosphate'>B9H</scene>, <scene name='pdbligand=BGH:[(2~{R},3~{R},4~{R},5~{R})-5-(2-azanyl-7-ethanoyl-6-oxidanylidene-1,8-dihydropurin-9-yl)-4-methoxy-3-oxidanyl-oxolan-2-yl]methyl+dihydrogen+phosphate'>BGH</scene>, <scene name='pdbligand=E7G:7-ethyl,+guanosine-5-monophosphate'>E7G</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=I4U:4-isopropyl,+uridine-5-monophosphate'>I4U</scene>, <scene name='pdbligand=M7A:7-methyl,+adenosine-5-monophosphate'>M7A</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=N:ANY+5-MONOPHOSPHATE+NUCLEOTIDE'>N</scene>, <scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=P4U:4-propyl,+uridine-5-monophosphate'>P4U</scene>, <scene name='pdbligand=P7G:7-propyl,+guanosine-5-monophosphate'>P7G</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=UR3:3-METHYLURIDINE-5-MONOPHOSHATE'>UR3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ir3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ir3 OCA], [https://pdbe.org/8ir3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ir3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ir3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ir3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL12_HUMAN RL12_HUMAN] Binds directly to 26S ribosomal RNA (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 A. 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.


Authors:  
Visualizing the nucleoplasmic maturation of human pre-60S ribosomal particles.,Zhang Y, Liang X, Luo S, Chen Y, Li Y, Ma C, Li N, Gao N Cell Res. 2023 Jul 25. doi: 10.1038/s41422-023-00853-9. PMID:37491604<ref>PMID:37491604</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8ir3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gao N]]
[[Category: Zhang Y]]

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