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[[Image: | ==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 [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EGV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MM:(1S)-1-CARBOXY-N,N,N-TRIMETHYL-3-(METHYLSULFANYL)PROPAN-1-AMINIUM'>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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nxc|2nxc]], [[2nxe|2nxe]], [[2nxj|2nxj]], [[2nxn|2nxn]], [[3cju|3cju]], [[3cjs|3cjs]], [[3cjr|3cjr]], [[3cjq|3cjq]], [[3cjt|3cjt]], [[1ufk|1ufk]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prmA, TTHA0656 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]), rplK, rpl11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</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=3egv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3egv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3egv RCSB], [http://www.ebi.ac.uk/pdbsum/3egv PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. [[http://www.uniprot.org/uniprot/RL11_THETH RL11_THETH]] This protein binds directly to 23S ribosomal RNA (By similarity). | |||
== 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/chain_selection.php?pdb_ID=2ata 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> | |||
==See Also== | ==See Also== | ||
*[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]] | *[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Dahlberg, A E | [[Category: Dahlberg, A E]] | ||
[[Category: Demirci, H | [[Category: Demirci, H]] | ||
[[Category: Gregory, S T | [[Category: Gregory, S T]] | ||
[[Category: Jogl, G | [[Category: Jogl, G]] | ||
[[Category: Methylation]] | [[Category: Methylation]] | ||
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
Revision as of 01:53, 25 December 2014
Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11
Structural highlights
Function[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. [RL11_THETH] This protein binds directly to 23S ribosomal RNA (By similarity). 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 PubMedRibosomal 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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