5xj2

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'''Unreleased structure'''
 
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The entry 5xj2 is ON HOLD
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==Structure of spRlmCD with U747 RNA==
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<StructureSection load='5xj2' size='340' side='right'caption='[[5xj2]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xj2]] is a 5 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=5XJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XJ2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xj2 OCA], [https://pdbe.org/5xj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xj2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xj2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y1029_STRPN Y1029_STRPN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RlmCD has recently been identified as the S-adenosyl methionine (SAM)-dependent methyltransferase responsible for the formation of m5U at U747 and U1939 of 23S ribosomal RNA in Streptococcus pneumoniae. In this research, we determine the high-resolution crystal structures of apo-form RlmCD and its complex with SAH. Using an in-vitro methyltransferase assay, we reveal the crucial residues for its catalytic functions. Furthermore, structural comparison between RlmCD and its structural homologue RumA, which only catalyzes the m5U1939 in Escherichia coli, implicates that a unique long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity. Its significance in the enzyme activity of RlmCD is further confirmed by in-vitro methyltransferase assay.
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Authors: Jiang, Y., Gong, Q.
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Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD.,Jiang Y, Li F, Wu J, Shi Y, Gong Q PLoS One. 2017 Sep 26;12(9):e0185226. doi: 10.1371/journal.pone.0185226., eCollection 2017. PMID:28949991<ref>PMID:28949991</ref>
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Description: Structure of spRlmCD with U747 RNA
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Jiang, Y]]
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<div class="pdbe-citations 5xj2" style="background-color:#fffaf0;"></div>
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[[Category: Gong, Q]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus pneumoniae TIGR4]]
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[[Category: Gong Q]]
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[[Category: Jiang Y]]

Current revision

Structure of spRlmCD with U747 RNA

PDB ID 5xj2

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