View source for 5gra


==Crystal structure of TrmJ from Z. mobilis ZM4==
<StructureSection load='5gra' size='340' side='right' caption='[[5gra]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gra]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymmo Zymmo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GRA FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trmJ, ZMO1203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264203 ZYMMO])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(cytidine(32)/uridine(32)-2'-O)-methyltransferase tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.200 2.1.1.200] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gra OCA], [http://pdbe.org/5gra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gra RCSB], [http://www.ebi.ac.uk/pdbsum/5gra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gra ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q5NN83_ZYMMO Q5NN83_ZYMMO]] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.[RuleBase:RU362024] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The tRNA methyltransferase J (TrmJ) and D (TrmD) catalyze the transferring reaction of a methyl group to the tRNA anticodon loop. They commonly have the N-terminal domain (NTD) and the C-terminal domain (CTD). Whereas two monomeric CTDs symmetrically interact with a dimeric NTD in TrmD, a CTD dimer has exhibited an asymmetric interaction with the NTD dimer in the presence of a product. The elucidated apo-structure of the full-length TrmJ from Zymomonas mobilis ZM4 shows a dimeric CTD that asymmetrically interacts with the NTD dimer, thereby distributing non-symmetrical potential charge on the both side of the protein surface. Comparison with the product-bound structures reveals a local re-orientation of the two arginine-containing loop at the active site, which interacts with the product. Further, the CTD dimers have diverse orientations compared to the NTD dimers, suggesting their flexibility. These data indicate that an asymmetric interaction between the NTD dimer and the CTD dimer is a common structural feature among TrmJ proteins, regardless of the presence of a substrate or a product.

An asymmetric dimeric structure of TrmJ tRNA methyltransferase from Zymomonas mobilis with a flexible C-terminal dimer.,Gu DH, Park MY, Kim JS Biochem Biophys Res Commun. 2017 Jun 24;488(2):407-412. doi:, 10.1016/j.bbrc.2017.05.068. Epub 2017 May 12. PMID:28506829<ref>PMID:28506829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gra" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Zymmo]]
[[Category: Gu, D H]]
[[Category: Kim, J S]]
[[Category: Methyltransferase]]
[[Category: Transferase]]
[[Category: Trmj]]
[[Category: Trna]]