2j37: Difference between revisions
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==MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS== | ==MODEL OF MAMMALIAN SRP BOUND TO 80S RNCS== | ||
<StructureSection load='2j37' size='340' side='right' caption='[[2j37]], [[Resolution|resolution]] 8.00Å' scene=''> | <StructureSection load='2j37' size='340' side='right' caption='[[2j37]], [[Resolution|resolution]] 8.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j37]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_sp. Canis sp.], [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2j37]] is a 8 chain structure with sequence from [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], [http://en.wikipedia.org/wiki/Triticum_sp. Triticum sp.] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J37 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dul|1dul]], [[1hq1|1hq1]], [[1p85|1p85]], [[1p86|1p86]], [[2aw4|2aw4]], [[2awb|2awb]], [[2j28|2j28]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dul|1dul]], [[1hq1|1hq1]], [[1p85|1p85]], [[1p86|1p86]], [[2aw4|2aw4]], [[2awb|2awb]], [[2j28|2j28]]</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=2j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j37 OCA], [http://pdbe.org/2j37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j37 RCSB], [http://www.ebi.ac.uk/pdbsum/2j37 PDBsum]</span></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=2j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j37 OCA], [http://pdbe.org/2j37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j37 RCSB], [http://www.ebi.ac.uk/pdbsum/2j37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j37 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SRP54_CANFA SRP54_CANFA]] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein) | [[http://www.uniprot.org/uniprot/SRP54_CANFA SRP54_CANFA]] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/2j37_consurf.spt"</scriptWhenChecked> | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 08:34, 8 March 2018
MODEL OF MAMMALIAN SRP BOUND TO 80S RNCSMODEL OF MAMMALIAN SRP BOUND TO 80S RNCS
Structural highlights
Function[SRP54_CANFA] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMembrane 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
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