View source for 5zth


==Crystal structure of spRlmCD with U1939loop RNA at 3.24 angstrom==
<StructureSection load='5zth' size='340' side='right'caption='[[5zth]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zth]] is a 2 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=5ZTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZTH 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]] 3.24&#8491;</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=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=5zth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zth OCA], [https://pdbe.org/5zth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zth RCSB], [https://www.ebi.ac.uk/pdbsum/5zth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zth ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1029_STRPN Y1029_STRPN] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30388185</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zth" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae TIGR4]]
[[Category: Jiang YY]]
[[Category: Yu HL]]