6lss
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Cryo-EM structure of a pre-60S ribosomal subunit - state preA== |
| - | <StructureSection load='6lss' size='340' side='right'caption='[[6lss]]' scene=''> | + | <StructureSection load='6lss' size='340' side='right'caption='[[6lss]], [[Resolution|resolution]] 3.23Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6lss]] 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=6LSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LSS FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.23Å</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=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=6MZ:N6-METHYLADENOSINE-5-MONOPHOSPHATE'>6MZ</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=B8H:[(2~{R},3~{S},4~{R},5~{S})-5-[1-methyl-2,4-bis(oxidanylidene)pyrimidin-5-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B8H</scene>, <scene name='pdbligand=B8K:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-7-ethanoyl-6-oxidanylidene-1,8-dihydropurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B8K</scene>, <scene name='pdbligand=B8Q:[(2~{R},3~{S},4~{R},5~{R})-5-(4-azanyl-3-methyl-2-oxidanylidene-4~{H}-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B8Q</scene>, <scene name='pdbligand=B8T:[(2~{R},3~{S},4~{R},5~{R})-5-[4-(methylamino)-2-oxidanylidene-pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B8T</scene>, <scene name='pdbligand=B8W:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-methoxy-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B8W</scene>, <scene name='pdbligand=B9B:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-propoxy-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>B9B</scene>, <scene name='pdbligand=B9H:[(2~{R},3~{R},4~{R},5~{R})-5-(4-azanyl-2-oxidanylidene-3-propyl-4~{H}-pyrimidin-1-yl)-4-methoxy-3-oxidanyl-oxolan-2-yl]methyl+dihydrogen+phosphate'>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=E6G:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-ethoxy-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>E6G</scene>, <scene name='pdbligand=E7G:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-7-ethyl-6-oxidanylidene-1,8-dihydropurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>E7G</scene>, <scene name='pdbligand=I4U:[(2~{R},3~{S},4~{R},5~{R})-3,4-bis(oxidanyl)-5-(2-oxidanylidene-4-propan-2-yloxy-pyrimidin-1-yl)oxolan-2-yl]methyl+dihydrogen+phosphate'>I4U</scene>, <scene name='pdbligand=M7A:[(2~{R},3~{S},4~{R},5~{R})-5-(6-azanyl-7-methyl-8~{H}-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>M7A</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MHG:[(2~{R},3~{S},4~{R},5~{R})-5-[2-(methylamino)-7-[(3~{S})-3-methylpentyl]-6-oxidanylidene-1,8-dihydropurin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>MHG</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:[(2~{R},3~{S},4~{R},5~{R})-3,4-bis(oxidanyl)-5-(2-oxidanylidene-4-propoxy-pyrimidin-1-yl)oxolan-2-yl]methyl+dihydrogen+phosphate'>P4U</scene>, <scene name='pdbligand=P7G:[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanylidene-7-propyl-3,8-dihydropurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+dihydrogen+phosphate'>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=6lss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lss OCA], [https://pdbe.org/6lss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lss RCSB], [https://www.ebi.ac.uk/pdbsum/6lss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lss ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IF6_HUMAN IF6_HUMAN] Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm (PubMed:10085284, PubMed:14654845, PubMed:21536732, PubMed:32669547). Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. 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 a RACK1 (RACK1)-dependent protein kinase C activity (PubMed:10085284, PubMed:14654845, PubMed:21536732). In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (By similarity). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (PubMed:17507929). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (By similarity).[HAMAP-Rule:MF_03132]<ref>PMID:10085284</ref> <ref>PMID:14654845</ref> <ref>PMID:17507929</ref> <ref>PMID:21536732</ref> <ref>PMID:32669547</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ribosome biogenesis is an elaborate and energetically expensive program that involve two hundred protein factors in eukaryotes. Nuclear export of pre-ribosomal particles is one central step which also serves as an internal structural checkpoint to ensure the proper completion of nuclear assembly events. Here we present four structures of human pre-60S particles isolated through a nuclear export factor NMD3, representing assembly stages immediately before and after nuclear export. These structures reveal locations of a dozen of human factors, including an uncharacterized factor TMA16 localized between the 5S RNA and the P0 stalk. Comparison of these structures shows a progressive maturation for the functional regions, such as peptidyl transferase centre and peptide exit tunnel, and illustrate a sequence of factor-assisted rRNA maturation events. These data facilitate our understanding of the global conservation of ribosome assembly in eukaryotes and species-specific features of human assembly factors. | ||
| + | |||
| + | Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.,Liang X, Zuo MQ, Zhang Y, Li N, Ma C, Dong MQ, Gao N Nat Commun. 2020 Jul 15;11(1):3542. doi: 10.1038/s41467-020-17237-x. PMID:32669547<ref>PMID:32669547</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6lss" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]] | ||
| + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | ||
| + | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
| + | *[[Ribosome biogenesis protein 3D structures|Ribosome biogenesis protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Dong M]] |
| + | [[Category: Gao N]] | ||
| + | [[Category: Li N]] | ||
| + | [[Category: Liang X]] | ||
| + | [[Category: Ma C]] | ||
| + | [[Category: Zhang Y]] | ||
| + | [[Category: Zuo M]] | ||
Current revision
Cryo-EM structure of a pre-60S ribosomal subunit - state preA
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Categories: Homo sapiens | Large Structures | Dong M | Gao N | Li N | Liang X | Ma C | Zhang Y | Zuo M
