1j1u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1j1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j1u, resolution 1.95&Aring;" /> '''Crystal structure of...)
Current revision (23:40, 27 December 2023) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1j1u.gif|left|200px]]<br /><applet load="1j1u" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1j1u, resolution 1.95&Aring;" />
 
-
'''Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine'''<br />
 
-
==Overview==
+
==Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine==
-
The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do, not cross-react with their bacterial counterparts. This 'orthogonal', condition is essential for using the archaeal pair to expand the bacterial, genetic code. In this study, the structure of the Methanococcus jannaschii, TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner, using different residues. These diverse tRNA recognition modes form the, basis for the orthogonality. The common tRNA(Tyr) identity determinants, (the discriminator, A73 and the anticodon residues) are also recognized in, manners different from those of the bacterial TyrRS. Based on this, finding, we created a mutant TyrRS that aminoacylates the amber suppressor, tRNA with C34 65 times more efficiently than does the wild-type enzyme.
+
<StructureSection load='1j1u' size='340' side='right'caption='[[1j1u]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1j1u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J1U FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene></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=1j1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1u OCA], [https://pdbe.org/1j1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j1u RCSB], [https://www.ebi.ac.uk/pdbsum/1j1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j1u ProSAT], [https://www.topsan.org/Proteins/RSGI/1j1u TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SYY_METJA SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</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/j1/1j1u_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=1j1u ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do not cross-react with their bacterial counterparts. This 'orthogonal' condition is essential for using the archaeal pair to expand the bacterial genetic code. In this study, the structure of the Methanococcus jannaschii TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner using different residues. These diverse tRNA recognition modes form the basis for the orthogonality. The common tRNA(Tyr) identity determinants (the discriminator, A73 and the anticodon residues) are also recognized in manners different from those of the bacterial TyrRS. Based on this finding, we created a mutant TyrRS that aminoacylates the amber suppressor tRNA with C34 65 times more efficiently than does the wild-type enzyme.
-
==About this Structure==
+
Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion.,Kobayashi T, Nureki O, Ishitani R, Yaremchuk A, Tukalo M, Cusack S, Sakamoto K, Yokoyama S Nat Struct Biol. 2003 Jun;10(6):425-32. PMID:12754495<ref>PMID:12754495</ref>
-
1J1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG and TYR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J1U OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion., Kobayashi T, Nureki O, Ishitani R, Yaremchuk A, Tukalo M, Cusack S, Sakamoto K, Yokoyama S, Nat Struct Biol. 2003 Jun;10(6):425-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12754495 12754495]
+
</div>
-
[[Category: Methanocaldococcus jannaschii]]
+
<div class="pdbe-citations 1j1u" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Tyrosine--tRNA ligase]]
+
-
[[Category: Cusack, S.]]
+
-
[[Category: Ishitani, R.]]
+
-
[[Category: Kobayashi, T.]]
+
-
[[Category: Nureki, O.]]
+
-
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+
-
[[Category: Sakamoto, K.]]
+
-
[[Category: Tukalo, M.]]
+
-
[[Category: Yokoyama, S.]]
+
-
[[Category: MG]]
+
-
[[Category: TYR]]
+
-
[[Category: aminoacyl-trna synthetase]]
+
-
[[Category: ligase]]
+
-
[[Category: riken structural genomics/proteomics initiative]]
+
-
[[Category: rsgi]]
+
-
[[Category: structural genomics]]
+
-
[[Category: trna]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:52:05 2007''
+
==See Also==
 +
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 +
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Methanocaldococcus jannaschii]]
 +
[[Category: Cusack S]]
 +
[[Category: Ishitani R]]
 +
[[Category: Kobayashi T]]
 +
[[Category: Nureki O]]
 +
[[Category: Sakamoto K]]
 +
[[Category: Tukalo M]]
 +
[[Category: Yokoyama S]]

Current revision

Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine

PDB ID 1j1u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools