View source for 4cng


==Crystal structure of Sulfolobus acidocaldarius TrmJ in complex with S-adenosyl-L-Homocysteine==
<StructureSection load='4cng' size='340' side='right'caption='[[4cng]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CNG 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]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4cng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cng OCA], [https://pdbe.org/4cng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cng RCSB], [https://www.ebi.ac.uk/pdbsum/4cng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cng ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRMJ_SULAC TRMJ_SULAC] Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA. Is specific for cytidine.<ref>PMID:24951554</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 2'-O-methylation of the nucleoside at position 32 of tRNA is found in organisms belonging to the three domains of life. Unrelated enzymes catalyzing this modification in Bacteria (TrmJ) and Eukarya (Trm7) have already been identified, but until now, no information is available for the archaeal enzyme. In this work we have identified the methyltransferase of the archaeon Sulfolobus acidocaldarius responsible for the 2'-O-methylation at position 32. This enzyme is a homolog of the bacterial TrmJ. Remarkably, both enzymes have different specificities for the nature of the nucleoside at position 32. While the four canonical nucleosides are substrates of the Escherichia coli enzyme, the archaeal TrmJ can only methylate the ribose of a cytidine. Moreover, the two enzymes recognize their tRNA substrates in a different way. We have solved the crystal structure of the catalytic domain of both enzymes to gain better understanding of these differences at a molecular level.

Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates.,Somme J, Van Laer B, Roovers M, Steyaert J, Versees W, Droogmans L RNA. 2014 Jun 20. PMID:24951554<ref>PMID:24951554</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cng" style="background-color:#fffaf0;"></div>

==See Also==
*[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Droogmans L]]
[[Category: Roovers M]]
[[Category: Somme J]]
[[Category: Steyaert J]]
[[Category: Van Laer B]]
[[Category: Versees W]]