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==Crystal structure of Escherichia coli 16S rRNA methyltransferase RsmI in complex with AdoMet==
<StructureSection load='5hw4' size='340' side='right'caption='[[5hw4]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hw4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HW4 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]] 2.211&#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=5hw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hw4 OCA], [https://pdbe.org/5hw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hw4 RCSB], [https://www.ebi.ac.uk/pdbsum/5hw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hw4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RSMI_ECOLI RSMI_ECOLI] Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes.<ref>PMID:19965768</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RsmI and RsmH are conserved S-Adenosylmethionine (AdoMet)-dependent methyltransferases (MTases) that are responsible for the 2'-O-methylation and N4-methylation of C1402 in bacterial 16S rRNA, respectively. Methylation of m4Cm1402 plays a role in fine-tuning the shape and functions of the P-site to increase the decoding fidelity, and was recently found to contribute to the virulence of Staphylococcus aureus in host animals. Here we report the 2.20-A crystal structure of homodimeric RsmI from Escherichia coli in complex with the cofactor AdoMet. RsmI consists of an N-terminal putative RNA-binding domain (NTD) and a C-terminal catalytic domain (CTD) with a Rossmann-like fold, and belongs to the class III MTase family. AdoMet is specifically bound into a negatively charged deep pocket formed by both domains by making extensive contacts. Structure-based mutagenesis and isothermal titration calorimetry (ITC) assays revealed Asp100 and Ala124 are vital for AdoMet-binding. Although the overall fold of RsmI shows remarkable similarities to the characterized MTases involved in vitamin B12 biosynthesis, it exhibits a distinct charge distribution especially around the AdoMet-binding pocket because of different substrate specificity. The docking model of RsmI-AdoMet-RNA ternary complex suggested a possible base-flipping mechanism of the substrate RNA that has been observed in several known RNA MTases. Our structural and biochemical studies provide novel insights into the catalytic mechanism of C1402 methylation in 16S rRNA.

Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI.,Zhao M, Zhang H, Liu G, Wang L, Wang J, Gao Z, Dong Y, Zhang L, Gong Y PLoS One. 2016 Oct 6;11(10):e0163816. doi: 10.1371/journal.pone.0163816., eCollection 2016. PMID:27711192<ref>PMID:27711192</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hw4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Dong Y]]
[[Category: Gong Y]]
[[Category: Zhang H]]
[[Category: Zhao M]]