<table><tr><td colspan='2'>[[3j7r]] is a 86 chain structure with sequence from [http://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=4w26 4w26], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w27 4w27], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w28 4w28], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx0 1vx0], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx1 1vx1], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx2 1vx2] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j73 3j73]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J7R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3j7r]] is a 86 chain structure with sequence from [http://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=4w26 4w26], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w27 4w27], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4w28 4w28], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx0 1vx0], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx1 1vx1], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vx2 1vx2] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j73 3j73]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J7R FirstGlance]. <br>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
Revision as of 17:28, 6 March 2020
Structure of the translating mammalian ribosome-Sec61 complex
3j7r is a 86 chain structure with sequence from Sus scrofa. This structure supersedes the now removed PDB entries 4w26, 4w27, 4w28, 1vx0, 1vx1, 1vx2 and 3j73. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[RL34_PIG] Component of the large ribosomal subunit.[1] [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). [RL10_PIG] Component of the large ribosomal subunit. Plays a role in the formation of actively translating ribosomes. May play a role in the embryonic brain development.[UniProtKB:P27635] [B6V8C8_PIG] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122] [RACK1_PIG] Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (By similarity). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration (By similarity). Regulates internalization of the muscarinic receptor CHRM2 (PubMed:20976005). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity).[UniProtKB:P63244][2] [RS18_PIG] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). [RL21_PIG] Component of the large ribosomal subunit.[3] [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). [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).[4] [RL6_PIG] Component of the large ribosomal subunit.[5] [A0A480UVT3_PIG] Binds to the 23S rRNA.[RuleBase:RU000576]
Publication Abstract from PubMed
Cotranslational protein translocation is a universally conserved process for secretory and membrane protein biosynthesis. Nascent polypeptides emerging from a translating ribosome are either transported across or inserted into the membrane via the ribosome-bound Sec61 channel. Here, we report structures of a mammalian ribosome-Sec61 complex in both idle and translating states, determined to 3.4 and 3.9 A resolution. The data sets permit building of a near-complete atomic model of the mammalian ribosome, visualization of A/P and P/E hybrid-state tRNAs, and analysis of a nascent polypeptide in the exit tunnel. Unprecedented chemical detail is observed for both the ribosome-Sec61 interaction and the conformational state of Sec61 upon ribosome binding. Comparison of the maps from idle and translating complexes suggests how conformational changes to the Sec61 channel could facilitate translocation of a secreted polypeptide. The high-resolution structure of the mammalian ribosome-Sec61 complex provides a valuable reference for future functional and structural studies.
Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution.,Voorhees RM, Fernandez IS, Scheres SH, Hegde RS Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun , 12. PMID:24930395[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Voorhees RM, Fernandez IS, Scheres SH, Hegde RS. Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution. Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun , 12. PMID:24930395 doi:http://dx.doi.org/10.1016/j.cell.2014.05.024
↑ Reiner CL, McCullar JS, Kow RL, Le JH, Goodlett DR, Nathanson NM. RACK1 associates with muscarinic receptors and regulates M(2) receptor trafficking. PLoS One. 2010 Oct 20;5(10):e13517. doi: 10.1371/journal.pone.0013517. PMID:20976005 doi:10.1371/journal.pone.0013517
↑ Voorhees RM, Fernandez IS, Scheres SH, Hegde RS. Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution. Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun , 12. PMID:24930395 doi:http://dx.doi.org/10.1016/j.cell.2014.05.024
↑ Tio PH, Jong WW, Cardosa MJ. Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3. Virol J. 2005 Mar 25;2:25. PMID:15790424 doi:http://dx.doi.org/10.1186/1743-422X-2-25
↑ Voorhees RM, Fernandez IS, Scheres SH, Hegde RS. Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution. Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun , 12. PMID:24930395 doi:http://dx.doi.org/10.1016/j.cell.2014.05.024
↑ Voorhees RM, Fernandez IS, Scheres SH, Hegde RS. Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution. Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun , 12. PMID:24930395 doi:http://dx.doi.org/10.1016/j.cell.2014.05.024