5e71: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) from Thermococcus kodakarensis== | ==Crystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) from Thermococcus kodakarensis== | ||
<StructureSection load='5e71' size='340' side='right' caption='[[5e71]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5e71' size='340' side='right'caption='[[5e71]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e71]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E71 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e71]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E71 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e72|5e72]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e72|5e72]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK0981 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=5e71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e71 OCA], [http://pdbe.org/5e71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e71 RCSB], [http://www.ebi.ac.uk/pdbsum/5e71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e71 ProSAT]</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=5e71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e71 OCA], [http://pdbe.org/5e71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e71 RCSB], [http://www.ebi.ac.uk/pdbsum/5e71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e71 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| Line 16: | Line 17: | ||
</div> | </div> | ||
<div class="pdbe-citations 5e71" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5e71" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[TRNA methyltransferase|TRNA methyltransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Hirata, A]] | [[Category: Hirata, A]] | ||
[[Category: Nfld]] | [[Category: Nfld]] | ||
Revision as of 10:13, 19 February 2020
Crystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) from Thermococcus kodakarensisCrystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) from Thermococcus kodakarensis
Structural highlights
Publication Abstract from PubMedN2-methylguanosine is one of the most universal modified nucleosides required for proper function in transfer RNA (tRNA) molecules. In archaeal tRNA species, a specific S-adenosyl-L-methionine (SAM)-dependent tRNA methyltransferase (MTase), aTrm11, catalyzes formation of N2-methylguanosine and N2,N2-dimethylguanosine at position 10. Here, we report the first X-ray crystal structures of aTrm11 from Thermococcus kodakarensis (Tko), of the apo-form, and of its complex with SAM. The structures show that TkoTrm11 consists of three domains: an N-terminal ferredoxinlike domain (NFLD), THUMP domain and Rossmann-fold MTase (RFM) domain. A linker region connects the THUMP-NFLD and RFM domains. One SAM molecule is bound in the pocket of the RFM domain, suggesting that TkoTrm11 uses a catalytic mechanism similar to that of other tRNA MTases containing an RFM domain. Furthermore, the conformation of NFLD and THUMP domains in TkoTrm11 resembles that of other tRNA-modifying enzymes specifically recognizing the tRNA acceptor stem. Our docking model of TkoTrm11-SAM in complex with tRNA, combined with biochemical analyses and pre-existing evidence, provides insights into the substrate tRNA recognition mechanism: The THUMP domain recognizes a 3'-ACCA end, and the linker region and RFM domain recognize the T-stem, acceptor stem and V-loop of tRNA, thereby causing TkoTrm11 to specifically identify its methylation site. Structural and functional analyses of the archaeal tRNA m2G/m22G10 methyltransferase aTrm11 provide mechanistic insights into site specificity of a tRNA methyltransferase that contains common RNA-binding modules.,Hirata A, Nishiyama S, Tamura T, Yamauchi A, Hori H Nucleic Acids Res. 2016 Jun 20. pii: gkw561. PMID:27325738[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||