5eqj

From Proteopedia

(Difference between revisions)

Revision as of 15:15, 14 September 2016

Crystal structure of the two-subunit tRNA m1A58 methyltransferase from Saccharomyces cerevisiae

Structural highlights

5eqj is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5erg
Activity:	tRNA (adenine(58)-N(1))-methyltransferase, with EC number 2.1.1.220
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRM6_YEAST] Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. Binds RNA. Also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.^[1] ^[2] ^[3] [TRM61_YEAST] Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.^[4] ^[5] ^[6]

Publication Abstract from PubMed

The N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal beta-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae.

Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.,Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X Sci Rep. 2016 Sep 1;6:32562. doi: 10.1038/srep32562. PMID:27582183^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Anderson J, Phan L, Hinnebusch AG. The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5173-8. PMID:10779558 doi:http://dx.doi.org/10.1073/pnas.090102597
↑ Garcia-Barrio MT, Naranda T, Vazquez de Aldana CR, Cuesta R, Hinnebusch AG, Hershey JW, Tamame M. GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3. Genes Dev. 1995 Jul 15;9(14):1781-96. PMID:7542616
↑ Anderson J, Phan L, Cuesta R, Carlson BA, Pak M, Asano K, Bjork GR, Tamame M, Hinnebusch AG. The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev. 1998 Dec 1;12(23):3650-62. PMID:9851972
↑ Anderson J, Phan L, Hinnebusch AG. The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5173-8. PMID:10779558 doi:http://dx.doi.org/10.1073/pnas.090102597
↑ Cuesta R, Hinnebusch AG, Tamame M. Identification of GCD14 and GCD15, novel genes required for translational repression of GCN4 mRNA in Saccharomyces cerevisiae. Genetics. 1998 Mar;148(3):1007-20. PMID:9539420
↑ Anderson J, Phan L, Cuesta R, Carlson BA, Pak M, Asano K, Bjork GR, Tamame M, Hinnebusch AG. The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev. 1998 Dec 1;12(23):3650-62. PMID:9851972
↑ Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X. Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae. Sci Rep. 2016 Sep 1;6:32562. doi: 10.1038/srep32562. PMID:27582183 doi:http://dx.doi.org/10.1038/srep32562

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5eqj"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5eqj is ON HOLD  until Paper Publication
+==Crystal structure of the two-subunit tRNA m1A58 methyltransferase from Saccharomyces cerevisiae==
+<StructureSection load='5eqj' size='340' side='right' caption='[[5eqj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5eqj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EQJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EQJ FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5erg|5erg]]</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA_(adenine(58)-N(1))-methyltransferase tRNA (adenine(58)-N(1))-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.220 2.1.1.220] </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=5eqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eqj OCA], [http://pdbe.org/5eqj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eqj RCSB], [http://www.ebi.ac.uk/pdbsum/5eqj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eqj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TRM6_YEAST TRM6_YEAST]] Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. Binds RNA. Also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.<ref>PMID:10779558</ref> <ref>PMID:7542616</ref> <ref>PMID:9851972</ref>  [[http://www.uniprot.org/uniprot/TRM61_YEAST TRM61_YEAST]] Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.<ref>PMID:10779558</ref> <ref>PMID:9539420</ref> <ref>PMID:9851972</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal beta-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae.
-Authors: Zhu, Y., Wang, M., Wang, C., Fan, X., Jiang, X., Teng, M., Li, X.
+Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.,Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X Sci Rep. 2016 Sep 1;6:32562. doi: 10.1038/srep32562. PMID:27582183<ref>PMID:27582183</ref>
-Description: Crystal structure of the two-subunit tRNA m1A58 methyltransferase from Saccharomyces cerevisiae
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wang, M]]
+<div class="pdbe-citations 5eqj" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Fan, X]]
 [[Category: Jiang, X]]
-[[Category: Teng, M]]
-[[Category: Zhu, Y]]
 [[Category: Li, X]]
+[[Category: Teng, M]]
 [[Category: Wang, C]]
-[[Category: Fan, X]]
+[[Category: Wang, M]]
+[[Category: Zhu, Y]]
+[[Category: Complex]]
+[[Category: Methyltransferase]]
+[[Category: Transferase]]
+[[Category: Trna]]

5eqj

From Proteopedia

Revision as of 15:15, 14 September 2016

Crystal structure of the two-subunit tRNA m1A58 methyltransferase from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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