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| | <StructureSection load='4cnd' size='340' side='right'caption='[[4cnd]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4cnd' size='340' side='right'caption='[[4cnd]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cnd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CND FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cnd]] 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=4CND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CND FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cne|4cne]]</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=4cnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnd OCA], [https://pdbe.org/4cnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cnd RCSB], [https://www.ebi.ac.uk/pdbsum/4cnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnd ProSAT]</span></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=4cnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnd OCA], [http://pdbe.org/4cnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cnd RCSB], [http://www.ebi.ac.uk/pdbsum/4cnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRMJ_ECOLI TRMJ_ECOLI]] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. | + | [[https://www.uniprot.org/uniprot/TRMJ_ECOLI TRMJ_ECOLI]] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[TRNA methyltransferase|TRNA methyltransferase]] | + | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Droogmans, L]] | + | [[Category: Droogmans L]] |
| - | [[Category: Laer, B Van]]
| + | [[Category: Roovers M]] |
| - | [[Category: Roovers, M]] | + | [[Category: Somme J]] |
| - | [[Category: Somme, J]] | + | [[Category: Steyaert J]] |
| - | [[Category: Steyaert, J]] | + | [[Category: Van Laer B]] |
| - | [[Category: Versees, W]] | + | [[Category: Versees W]] |
| - | [[Category: Spout]] | + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
[TRMJ_ECOLI] Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Somme J, Van Laer B, Roovers M, Steyaert J, Versees W, Droogmans L. Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates. RNA. 2014 Jun 20. PMID:24951554 doi:http://dx.doi.org/10.1261/rna.044503.114
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