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5lzs

From Proteopedia

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Current revision

Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B

5lzs, resolution 3.31Å

Structural highlights

5lzs is a 10 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.31Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G1U7M4_RABIT

Publication Abstract from PubMed

In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factorGTPase complexes representing intermediates of translation elongation (aminoacyl-tRNAeEF1A), termination (eRF1eRF3), and ribosome rescue (PelotaHbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factorGTPase complex to ensure translational fidelity.

Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.,Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS Cell. 2016 Nov 17;167(5):1229-1240.e15. doi: 10.1016/j.cell.2016.10.046. PMID:27863242^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS. Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Cell. 2016 Nov 17;167(5):1229-1240.e15. doi: 10.1016/j.cell.2016.10.046. PMID:27863242 doi:http://dx.doi.org/10.1016/j.cell.2016.10.046

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lzs"

@@ Line 3: / Line 3: @@
 <SX load='5lzs' size='340' side='right' viewer='molstar' caption='[[5lzs]], [[Resolution|resolution]] 3.31&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lzs]] is a 86 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LZS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lzs]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LZS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7C4:(2~{S})-~{N}-[(2~{R})-1-[[(3~{S},6~{S},8~{S},12~{S},13~{R},16~{S},17~{R},20~{S},23~{S})-13-[(2~{S})-BUTAN-2-YL]-20-[(4-METHOXYPHENYL)METHYL]-6,17,21-TRIMETHYL-3-(2-METHYLPROPYL)-12-OXIDANYL-2,5,7,10,15,19,22-HEPTAKIS(OXIDANYLIDENE)-8-PROPAN-2-YL-9,18-DIOXA-1,4,14,21-TETRAZABICYCLO[21.3.0]HEXACOSAN-16-YL]AMINO]-4-METHYL-1-OXIDANYLIDENE-PENTAN-2-YL]-~{N}-METHYL-1-[(2~{S})-2-OXIDANYLPROPANOYL]PYRROLIDINE-2-CARBOXAMIDE'>7C4</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <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]] 3.31&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7C4:(2~{S})-~{N}-[(2~{R})-1-[[(3~{S},6~{S},8~{S},12~{S},13~{R},16~{S},17~{R},20~{S},23~{S})-13-[(2~{S})-BUTAN-2-YL]-20-[(4-METHOXYPHENYL)METHYL]-6,17,21-TRIMETHYL-3-(2-METHYLPROPYL)-12-OXIDANYL-2,5,7,10,15,19,22-HEPTAKIS(OXIDANYLIDENE)-8-PROPAN-2-YL-9,18-DIOXA-1,4,14,21-TETRAZABICYCLO[21.3.0]HEXACOSAN-16-YL]AMINO]-4-METHYL-1-OXIDANYLIDENE-PENTAN-2-YL]-~{N}-METHYL-1-[(2~{S})-2-OXIDANYLPROPANOYL]PYRROLIDINE-2-CARBOXAMIDE'>7C4</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lzs OCA], [http://pdbe.org/5lzs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lzs RCSB], [http://www.ebi.ac.uk/pdbsum/5lzs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lzs 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=5lzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lzs OCA], [https://pdbe.org/5lzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lzs RCSB], [https://www.ebi.ac.uk/pdbsum/5lzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lzs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/U3KPD5_RABIT U3KPD5_RABIT]] Binds to the 23S rRNA.[RuleBase:RU000576] [[http://www.uniprot.org/uniprot/G1SS70_RABIT G1SS70_RABIT]] May play a role during erythropoiesis through regulation of transcription factor DDIT3.[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/EF1A1_RABIT EF1A1_RABIT]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (By similarity).
+[https://www.uniprot.org/uniprot/G1U7M4_RABIT G1U7M4_RABIT]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Receptor for activated protein kinase C 1|Receptor for activated protein kinase C 1]]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+*[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]]
 == References ==
 <references/>
@@ Line 28: / Line 29: @@
 [[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Brown, A]]
+[[Category: Brown A]]
-[[Category: Hegde, R S]]
+[[Category: Hegde RS]]
-[[Category: Murray, J]]
+[[Category: Murray J]]
-[[Category: Ramakrishnan, V]]
+[[Category: Ramakrishnan V]]
-[[Category: Shao, S]]
+[[Category: Shao S]]
-[[Category: Taunton, J]]
+[[Category: Taunton J]]
-[[Category: Elongation]]
-[[Category: Ribosome]]
-[[Category: Translation]]

5lzs

From Proteopedia

Current revision

Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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