2j37: Difference between revisions

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-[[Image:2j37.gif|left|200px]]
- {{Structure
+==MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS==
-|PDB= 2j37 |SIZE=350|CAPTION= <scene name='initialview01'>2j37</scene>, resolution 8.0&Aring;
+<SX load='2j37' size='340' side='right' viewer='molstar' caption='[[2j37]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
+<table><tr><td colspan='2'>[[2j37]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_sp. Canis sp.], [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Triticum_sp. Triticum sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J37 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j37 OCA], [https://pdbe.org/2j37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j37 RCSB], [https://www.ebi.ac.uk/pdbsum/2j37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j37 ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j37 OCA], [http://www.ebi.ac.uk/pdbsum/2j37 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j37 RCSB]</span>
+[https://www.uniprot.org/uniprot/O81229_MAIZE O81229_MAIZE] Binds to 23S rRNA.[ARBA:ARBA00002500]
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/2j37_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j37 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.
-'''MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS'''
+Following the signal sequence from ribosomal tunnel exit to signal recognition particle.,Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R Nature. 2006 Nov 23;444(7118):507-11. Epub 2006 Oct 29. PMID:17086193<ref>PMID:17086193</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2j37" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.
+*[[Ribosomal protein L23|Ribosomal protein L23]]
+*[[Ribosomal protein L31|Ribosomal protein L31]]
-==About this Structure==
+*[[Ribosomal protein L35|Ribosomal protein L35]]
-J37 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris], [http://en.wikipedia.org/wiki/Canis_sp. Canis sp.], [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J37 OCA].
+*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
+== References ==
-==Reference==
+<references/>
-Following the signal sequence from ribosomal tunnel exit to signal recognition particle., Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R, Nature. 2006 Nov 23;444(7118):507-11. Epub 2006 Oct 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17086193 17086193]
+__TOC__
-[[Category: Canis lupus familiaris]]
+</SX>
-[[Category: Canis sp.]]
+[[Category: Canis sp]]
 [[Category: Haloarcula marismortui]]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Triticum aestivum]]
+[[Category: Triticum sp]]
-[[Category: Becker, T.]]
+[[Category: Becker T]]
-[[Category: Beckmann, R.]]
+[[Category: Beckmann R]]
-[[Category: Blau, M.]]
+[[Category: Blau M]]
-[[Category: Halic, M.]]
+[[Category: Halic M]]
-[[Category: Mielke, T.]]
+[[Category: Mielke T]]
-[[Category: Pool, M R.]]
+[[Category: Pool MR]]
-[[Category: Sinning, I.]]
+[[Category: Sinning I]]
-[[Category: Wild, K.]]
+[[Category: Wild K]]
-[[Category: ribosome]]
-[[Category: srp]]
-[[Category: translation/rna]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:15 2008''