4jak: Difference between revisions

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-'''Unreleased structure'''
-The entry 4jak is ON HOLD
+==Crystal structure of tRNA (Um34/Cm34) methyltransferase TrmL from Escherichia coli==
+<StructureSection load='4jak' size='340' side='right'caption='[[4jak]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4jak]] is a 2 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=4JAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JAK 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&#8491;</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=4jak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jak OCA], [https://pdbe.org/4jak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jak RCSB], [https://www.ebi.ac.uk/pdbsum/4jak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jak ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRML_ECOLI TRML_ECOLI] Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. Recognition of the target requires a pyridine at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position 37.<ref>PMID:20855540</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Unlike other transfer RNAs (tRNA)-modifying enzymes from the SPOUT methyltransferase superfamily, the tRNA (Um34/Cm34) methyltransferase TrmL lacks the usual extension domain for tRNA binding and consists only of a SPOUT domain. Both the catalytic and tRNA recognition mechanisms of this enzyme remain elusive. By using tRNAs purified from an Escherichia coli strain with the TrmL gene deleted, we found that TrmL can independently catalyze the methyl transfer from S-adenosyl-L-methionine to and isoacceptors without the involvement of other tRNA-binding proteins. We have solved the crystal structures of TrmL in apo form and in complex with S-adenosyl-homocysteine and identified the cofactor binding site and a possible active site. Methyltransferase activity and tRNA-binding affinity of TrmL mutants were measured to identify residues important for tRNA binding of TrmL. Our results suggest that TrmL functions as a homodimer by using the conserved C-terminal half of the SPOUT domain for catalysis, whereas residues from the less-conserved N-terminal half of the other subunit participate in tRNA recognition.
-Authors: Liu, R.J., Zhou, M., Wang, E.D.
+The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL.,Liu RJ, Zhou M, Fang ZP, Wang M, Zhou XL, Wang ED Nucleic Acids Res. 2013 Jun 26. PMID:23804755<ref>PMID:23804755</ref>
-Description: Crystal structure of tRNA (Um34/Cm34) methyltransferase TrmL from Escherichia coli
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4jak" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Liu RJ]]
+[[Category: Wang ED]]
+[[Category: Zhou M]]