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| | ==Crystal structure of spRlmCD with U747 stemloop RNA== | | ==Crystal structure of spRlmCD with U747 stemloop RNA== |
| - | <StructureSection load='5zq8' size='340' side='right' caption='[[5zq8]], [[Resolution|resolution]] 2.18Å' scene=''> | + | <StructureSection load='5zq8' size='340' side='right'caption='[[5zq8]], [[Resolution|resolution]] 2.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zq8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZQ8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zq8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZQ8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MUM:'>MUM</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MUM:5-O-(dihydroxyphosphanyl)-5-methyl-5,6-dihydrouridine'>MUM</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">[[5zq0|5zq0]]</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=5zq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zq8 OCA], [https://pdbe.org/5zq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zq8 RCSB], [https://www.ebi.ac.uk/pdbsum/5zq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zq8 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SP_1029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</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=5zq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zq8 OCA], [http://pdbe.org/5zq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zq8 RCSB], [http://www.ebi.ac.uk/pdbsum/5zq8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zq8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Y1029_STRPN Y1029_STRPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strpn]] | + | [[Category: Large Structures]] |
| - | [[Category: Jiang, Y Y]]
| + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Yu, H L]]
| + | [[Category: Jiang YY]] |
| - | [[Category: 23s rna]]
| + | [[Category: Yu HL]] |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Ribosome]]
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| - | [[Category: Streptococcus pneumoniae]] | + | |
| - | [[Category: Transferase]] | + | |
| - | [[Category: Transferase-rna complex]] | + | |
| Structural highlights
Function
Y1029_STRPN
Publication Abstract from PubMed
Methyltransferase RlmCD was previously shown to be responsible for the introduction of C5 methylation at both U747 and U1939 of the 23S ribosomal RNA in Streptococcus pneumoniae. Intriguingly, its structural homologue, RumA, can only catalyze the methylation of U1939, while RlmC is the dedicated enzyme for m5U747 in Escherichia coli. In this study, we describe the structure of RlmCD in complex with its cofactor and the RNA substrate containing U747 at 2.00 A or U1939 at 3.10 A. We demonstrate that multiple structural features collaborate to establish the dual enzymatic activities of RlmCD. Of them, the side-chain rearrangement of F145 was observed to be an unusual mechanism through which RlmCD can discriminate between U747- and U1939-containing RNA substrate by switching the intermolecular aromatic stacking between protein and RNA on/off. An in-vitro methyltransferase assay and electrophoretic mobility shift assay were performed to validate these findings. Overall, our complex structures allow for a better understanding of the dual-functional mechanism of RlmCD, suggesting useful implications for the evolution of the RumA-type enzyme and the potential development of antibiotic drugs against S. pneumoniae.
Unveiling the structural features that determine the dual methyltransferase activities of Streptococcus pneumoniae RlmCD.,Jiang Y, Yu H, Li F, Cheng L, Zhu L, Shi Y, Gong Q PLoS Pathog. 2018 Nov 2;14(11):e1007379. doi: 10.1371/journal.ppat.1007379. PMID:30388185[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jiang Y, Yu H, Li F, Cheng L, Zhu L, Shi Y, Gong Q. Unveiling the structural features that determine the dual methyltransferase activities of Streptococcus pneumoniae RlmCD. PLoS Pathog. 2018 Nov 2;14(11):e1007379. doi: 10.1371/journal.ppat.1007379. PMID:30388185 doi:http://dx.doi.org/10.1371/journal.ppat.1007379
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