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New page: left|200px<br /><applet load="2nxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nxc, resolution 1.59Å" /> '''Apo-form of T. therm... |
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== | ==Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)== | ||
Bacterial ribosomal protein L11 is post-translationally trimethylated at | <StructureSection load='2nxc' size='340' side='right'caption='[[2nxc]], [[Resolution|resolution]] 1.59Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2nxc]] is a 1 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=2NXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NXC 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]] 1.59Å</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=2nxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nxc OCA], [https://pdbe.org/2nxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nxc RCSB], [https://www.ebi.ac.uk/pdbsum/2nxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nxc 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/nx/2nxc_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=2nxc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 A resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit. | |||
Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA.,Demirci H, Gregory ST, Dahlberg AE, Jogl G EMBO J. 2007 Jan 24;26(2):567-77. Epub 2007 Jan 11. PMID:17215866<ref>PMID:17215866</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2nxc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[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]] | |||
Latest revision as of 13:25, 30 August 2023
Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)
Structural highlights
FunctionPRMA_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 A resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit. Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA.,Demirci H, Gregory ST, Dahlberg AE, Jogl G EMBO J. 2007 Jan 24;26(2):567-77. Epub 2007 Jan 11. PMID:17215866[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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