2nxn: Difference between revisions
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<StructureSection load='2nxn' size='340' side='right'caption='[[2nxn]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2nxn' size='340' side='right'caption='[[2nxn]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nxn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2nxn]] is a 2 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=2NXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NXN FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=2nxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nxn OCA], [https://pdbe.org/2nxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nxn RCSB], [https://www.ebi.ac.uk/pdbsum/2nxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nxn ProSAT]</span></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=2nxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nxn OCA], [https://pdbe.org/2nxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nxn RCSB], [https://www.ebi.ac.uk/pdbsum/2nxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nxn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Ribosomal protein L11|Ribosomal protein L11]] | *[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]] | ||
*[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]] | *[[Ribosomal protein L11 methyltransferase|Ribosomal protein L11 methyltransferase]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Dahlberg | [[Category: Dahlberg AE]] | ||
[[Category: Demirci | [[Category: Demirci H]] | ||
[[Category: Gregory | [[Category: Gregory ST]] | ||
[[Category: Jogl | [[Category: Jogl G]] | ||
Latest revision as of 13:25, 30 August 2023
T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11
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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