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[[Image:2hsn.jpg|left|200px]]


{{Structure
==Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes==
|PDB= 2hsn |SIZE=350|CAPTION= <scene name='initialview01'>2hsn</scene>, resolution 2.20&Aring;
<StructureSection load='2hsn' size='340' side='right'caption='[[2hsn]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2hsn]] 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=2HSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSN FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= MES1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsn OCA], [https://pdbe.org/2hsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsn RCSB], [https://www.ebi.ac.uk/pdbsum/2hsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsn ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARC1_YEAST ARC1_YEAST] Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.<ref>PMID:11069915</ref> <ref>PMID:17131041</ref> <ref>PMID:8895587</ref> <ref>PMID:9659920</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/2hsn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2hsn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 A, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors.


'''Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes'''
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes.,Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:16914447<ref>PMID:16914447</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hsn" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 A, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors.
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2HSN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSN OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes., Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D, Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16914447 16914447]
[[Category: Methionine--tRNA ligase]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Basquin, J.]]
[[Category: Basquin J]]
[[Category: Koehler, C.]]
[[Category: Koehler C]]
[[Category: Simader, H.]]
[[Category: Simader H]]
[[Category: Suck, D.]]
[[Category: Suck D]]
[[Category: protein complex protein interaction gst-fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:21:07 2008''

Latest revision as of 13:01, 30 August 2023

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexesStructural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes

Structural highlights

2hsn 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 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARC1_YEAST Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.[1] [2] [3] [4]

Evolutionary Conservation

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

Publication Abstract from PubMed

The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 A, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors.

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes.,Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:16914447[5]

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

See Also

References

  1. ↑ Deinert K, Fasiolo F, Hurt EC, Simos G. Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem. 2001 Feb 23;276(8):6000-8. PMID:11069915 doi:10.1074/jbc.M008682200
  2. ↑ Golinelli-Cohen MP, Mirande M. Arc1p is required for cytoplasmic confinement of synthetases and tRNA. Mol Cell Biochem. 2007 Jun;300(1-2):47-59. PMID:17131041 doi:10.1007/s11010-006-9367-4
  3. ↑ Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the EMBO J. 1996 Oct 1;15(19):5437-48 PMID:8895587
  4. ↑ Simos G, Sauer A, Fasiolo F, Hurt EC. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol Cell. 1998 Jan;1(2):235-42. PMID:9659920 doi:10.1016/s1097-2765(00)80024-6
  5. ↑ Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:16914447 doi:10.1093/nar/gkl560

2hsn, resolution 2.20Å

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