View source for 5twj


==Crystal Structure of RlmH in Complex with S-Adenosylmethionine==
<StructureSection load='5twj' size='340' side='right'caption='[[5twj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5twj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TWJ 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]] 2.299&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=5twj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5twj OCA], [https://pdbe.org/5twj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5twj RCSB], [https://www.ebi.ac.uk/pdbsum/5twj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5twj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RLMH_ECOLI RLMH_ECOLI] Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes.<ref>PMID:18755835</ref> <ref>PMID:18755836</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Psi1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.

Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.,Koh CS, Madireddy R, Beane TJ, Zamore PD, Korostelev AA Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. PMID:28428565<ref>PMID:28428565</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5twj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Beane TJ]]
[[Category: Koh CS]]
[[Category: Korostelev AA]]
[[Category: Madireddy R]]
[[Category: Zamore PD]]