3egv: Difference between revisions
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New page: '''Unreleased structure''' The entry 3egv is ON HOLD Authors: Demirci, H., Gregory, S.T., Dahlberg, A.E., Jogl, G. Description: Ribosomal protein L11 methyltransferase (PrmA) in comple... |
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==Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11== | |||
<StructureSection load='3egv' size='340' side='right'caption='[[3egv]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3egv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3cju 3cju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EGV 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]] 1.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MM:N,N,N-TRIMETHYLMETHIONINE'>4MM</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=3egv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3egv OCA], [https://pdbe.org/3egv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3egv RCSB], [https://www.ebi.ac.uk/pdbsum/3egv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3egv 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/eg/3egv_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=3egv 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3egv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]] | |||
*[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Dahlberg AE]] | |||
[[Category: Demirci H]] | |||
[[Category: Gregory ST]] | |||
[[Category: Jogl G]] | |||
