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[[Image:2d3o.gif|left|200px]]<br /><applet load="2d3o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2d3o, resolution 3.35&Aring;" />
'''Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans'''<br />


==Overview==
==Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans==
This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 A, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.
<StructureSection load='2d3o' size='340' side='right'caption='[[2d3o]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2d3o]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</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=2d3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3o OCA], [https://pdbe.org/2d3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3o RCSB], [https://www.ebi.ac.uk/pdbsum/2d3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL23_DEIRA RL23_DEIRA] One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_01369]
== 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/d3/2d3o_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=2d3o ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2D3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA].
*[[Ribosomal protein L23|Ribosomal protein L23]]
 
*[[Ribosomal protein L24|Ribosomal protein L24]]
==Reference==
*[[Ribosomal protein L29|Ribosomal protein L29]]
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction., Schlunzen F, Wilson DN, Tian P, Harms JM, McInnes SJ, Hansen HA, Albrecht R, Buerger J, Wilbanks SM, Fucini P, Structure. 2005 Nov;13(11):1685-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16271892 16271892]
*[[Ribosome 3D structures|Ribosome 3D structures]]
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Albrecht, R.]]
[[Category: Albrecht R]]
[[Category: Buerger, J.]]
[[Category: Buerger J]]
[[Category: Fucini, P.]]
[[Category: Fucini P]]
[[Category: Hansen, H A.]]
[[Category: Hansen HA]]
[[Category: Harms, J M.]]
[[Category: Harms JM]]
[[Category: McInnes, S J.]]
[[Category: McInnes SJ]]
[[Category: Schluenzen, F.]]
[[Category: Schluenzen F]]
[[Category: Tian, P.]]
[[Category: Tian P]]
[[Category: Wilbanks, S M.]]
[[Category: Wilbanks SM]]
[[Category: Wilson, D N.]]
[[Category: Wilson DN]]
[[Category: 50s]]
[[Category: nascent chain]]
[[Category: protein folding]]
[[Category: ribosome]]
[[Category: srp]]
[[Category: trigger factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:05 2008''

Latest revision as of 16:46, 13 March 2024

Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radioduransStructure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans

Structural highlights

2d3o is a 5 chain structure with sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.35Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL23_DEIRA One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_01369]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2d3o, resolution 3.35Å

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