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<StructureSection load='2vdv' size='340' side='right'caption='[[2vdv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2vdv' size='340' side='right'caption='[[2vdv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vdv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VDV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vdv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vdu|2vdu]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(guanine(46)-N(7))-methyltransferase tRNA (guanine(46)-N(7))-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.33 2.1.1.33] </span></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=2vdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdv OCA], [https://pdbe.org/2vdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vdv RCSB], [https://www.ebi.ac.uk/pdbsum/2vdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdv OCA], [http://pdbe.org/2vdv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdv RCSB], [http://www.ebi.ac.uk/pdbsum/2vdv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRMB_YEAST TRMB_YEAST]] Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.[HAMAP-Rule:MF_03055]<ref>PMID:16387656</ref> <ref>PMID:17382321</ref>
[https://www.uniprot.org/uniprot/TRMB_YEAST TRMB_YEAST] Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.[HAMAP-Rule:MF_03055]<ref>PMID:16387656</ref> <ref>PMID:17382321</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vdv ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vdv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Loss of N7-methylguanosine (m7G) modification is involved in the recently discovered rapid tRNA degradation pathway. In yeast, this modification is catalyzed by the heterodimeric complex composed of a catalytic subunit Trm8 and a noncatalytic subunit Trm82. We have solved the crystal structure of Trm8 alone and in complex with Trm82. Trm8 undergoes subtle conformational changes upon Trm82 binding which explains the requirement of Trm82 for activity. Cocrystallization with the S-adenosyl-methionine methyl donor defines the putative catalytic site and a guanine binding pocket. Small-angle X-ray scattering in solution of the Trm8-Trm82 heterodimer in complex with tRNA(Phe) has enabled us to propose a low-resolution structure of the ternary complex which defines the tRNA binding mode of Trm8-Trm82 and the structural elements contributing to specificity.
Structure of the yeast tRNA m7G methylation complex.,Leulliot N, Chaillet M, Durand D, Ulryck N, Blondeau K, van Tilbeurgh H Structure. 2008 Jan;16(1):52-61. PMID:18184583<ref>PMID:18184583</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vdv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blondeau, K]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Chaillet, M]]
[[Category: Blondeau K]]
[[Category: Durand, D]]
[[Category: Chaillet M]]
[[Category: Leulliot, N]]
[[Category: Durand D]]
[[Category: Tilbeurgh, H Van]]
[[Category: Leulliot N]]
[[Category: Ulryck, N]]
[[Category: Ulryck N]]
[[Category: M7g]]
[[Category: Van Tilbeurgh H]]
[[Category: Methyltransferase]]
[[Category: Phosphorylation]]
[[Category: S-adenosyl-l-methionine]]
[[Category: Spout mt]]
[[Category: Transferase]]
[[Category: Trna]]
[[Category: Trna processing]]

Latest revision as of 10:07, 1 May 2024

Structure of trm8, m7G methylation enzymeStructure of trm8, m7G methylation enzyme

Structural highlights

2vdv is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRMB_YEAST Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.[HAMAP-Rule:MF_03055][1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Alexandrov A, Chernyakov I, Gu W, Hiley SL, Hughes TR, Grayhack EJ, Phizicky EM. Rapid tRNA decay can result from lack of nonessential modifications. Mol Cell. 2006 Jan 6;21(1):87-96. PMID:16387656 doi:http://dx.doi.org/S1097-2765(05)01731-4
  2. ↑ Matsumoto K, Toyooka T, Tomikawa C, Ochi A, Takano Y, Takayanagi N, Endo Y, Hori H. RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase (Trm8-Trm82 complex). FEBS Lett. 2007 Apr 17;581(8):1599-604. Epub 2007 Mar 16. PMID:17382321 doi:http://dx.doi.org/S0014-5793(07)00277-3

2vdv, resolution 2.30Å

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