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| | <SX load='3j7p' size='340' side='right' viewer='molstar' caption='[[3j7p]], [[Resolution|resolution]] 3.50Å' scene=''> | | <SX load='3j7p' size='340' side='right' viewer='molstar' caption='[[3j7p]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3j7p]] is a 82 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w21 4w21], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w22 4w22], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w23 4w23], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx3 1vx3], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx4 1vx4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx5 1vx5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j74 3j74]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J7P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j7p]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w21 4w21], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w22 4w22], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w23 4w23], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx3 1vx3], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx4 1vx4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx5 1vx5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j74 3j74]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J7P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3j7o|3j7o]], [[3j7q|3j7q]], [[3j7r|3j7r]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3j7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j7p OCA], [https://pdbe.org/3j7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j7p RCSB], [https://www.ebi.ac.uk/pdbsum/3j7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j7p ProSAT]</span></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=3j7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j7p OCA], [https://pdbe.org/3j7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j7p RCSB], [https://www.ebi.ac.uk/pdbsum/3j7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j7p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RSSA_PIG RSSA_PIG]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity).<ref>PMID:15790424</ref> [[https://www.uniprot.org/uniprot/RS18_PIG RS18_PIG]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). [[https://www.uniprot.org/uniprot/RL40_PIG RL40_PIG]] Ubiquitin: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 60S ribosomal protein L40: component of the 60S subunit of the ribosome (By similarity). [[https://www.uniprot.org/uniprot/RL11_PIG RL11_PIG]] Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). [[https://www.uniprot.org/uniprot/B6V8C8_PIG B6V8C8_PIG]] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122]
| + | [https://www.uniprot.org/uniprot/F2Z567_PIG F2Z567_PIG] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3j7p" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3j7p" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | + | *[[Ribosome 3D structures|Ribosome 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| - | [[Category: Fernandez, I S]] | + | [[Category: Fernandez IS]] |
| - | [[Category: Hegde, R S]] | + | [[Category: Hegde RS]] |
| - | [[Category: Scheres, S H.W]] | + | [[Category: Scheres SHW]] |
| - | [[Category: Voorhees, R M]] | + | [[Category: Voorhees RM]] |
| - | [[Category: Eef2]]
| + | |
| - | [[Category: Mammalian]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Sec61]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translocation]]
| + | |
