3cjq: Difference between revisions

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[[Image:3cjq.png|left|200px]]


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==Ribosomal protein L11 methyltransferase (PrmA) in complex with dimethylated ribosomal protein L11 in space group P212121==
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<StructureSection load='3cjq' size='340' side='right'caption='[[3cjq]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3cjq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CJQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MM:N,N-DIMETHYL-L-METHIONINE'>2MM</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
{{STRUCTURE_3cjq|  PDB=3cjq  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjq OCA], [https://pdbe.org/3cjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cjq RCSB], [https://www.ebi.ac.uk/pdbsum/3cjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cjq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRMA_THET8 PRMA_THET8] Methylates ribosomal protein L11; this reaction probably occurs before the protein is assembled into the ribosome. This function is dispensable for growth and thermostability.
== 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/cj/3cjq_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=3cjq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.


===Ribosomal protein L11 methyltransferase (PrmA) in complex with dimethylated ribosomal protein L11 in space group P212121===
Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.,Demirci H, Gregory ST, Dahlberg AE, Jogl G Structure. 2008 Jul;16(7):1059-66. PMID:18611379<ref>PMID:18611379</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3cjq" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18611379}}, adds the Publication Abstract to the page
*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18611379 is the PubMed ID number.
*[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]]
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== References ==
{{ABSTRACT_PUBMED_18611379}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
3CJQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJQ OCA].
[[Category: Large Structures]]
 
[[Category: Thermus thermophilus HB8]]
==Reference==
[[Category: Dahlberg AE]]
Multiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA Methyltransferase., Demirci H, Gregory ST, Dahlberg AE, Jogl G, Structure. 2008 Jul;16(7):1059-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18611379 18611379]
[[Category: Demirci H]]
[[Category: Protein complex]]
[[Category: Gregory ST]]
[[Category: Thermus thermophilus]]
[[Category: Jogl G]]
[[Category: Dahlberg, A E.]]
[[Category: Demirci, H.]]
[[Category: Gregory, S T.]]
[[Category: Jogl, G.]]
[[Category: Cytoplasm]]
[[Category: Multi-specific trimethylation]]
[[Category: Post-translational modification]]
[[Category: Ribonucleoprotein]]
[[Category: Ribosomal protein]]
[[Category: Rna-binding]]
[[Category: Rrna-binding]]
[[Category: S-adenosyl-l-methionine dependent methyltransferase]]
[[Category: Transferase/ribosomal protein complex]]
 
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