1zh6: Difference between revisions

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-[[Image:1zh6.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1zh6", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1zh6|  PDB=1zh6  |  SCENE=  }}
-'''Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine'''
+==Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine==
+<StructureSection load='1zh6' size='340' side='right'caption='[[1zh6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1zh6]] is a 1 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=1ZH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZH6 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4AF:4-ACETYL-L-PHENYLALANINE'>4AF</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=1zh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zh6 OCA], [https://pdbe.org/1zh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zh6 RCSB], [https://www.ebi.ac.uk/pdbsum/1zh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zh6 ProSAT]</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/zh/1zh6_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=1zh6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acid p-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.
-==Overview==
+Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase.,Turner JM, Graziano J, Spraggon G, Schultz PG J Am Chem Soc. 2005 Nov 2;127(43):14976-7. PMID:16248607<ref>PMID:16248607</ref>
-It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acid p-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-ZH6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZH6 OCA].
+</div>
+<div class="pdbe-citations 1zh6" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase., Turner JM, Graziano J, Spraggon G, Schultz PG, J Am Chem Soc. 2005 Nov 2;127(43):14976-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16248607 16248607]
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Methanocaldococcus jannaschii]]
-[[Category: Single protein]]
+[[Category: Graziano J]]
-[[Category: Tyrosine--tRNA ligase]]
+[[Category: Schultz PG]]
-[[Category: Graziano, J.]]
+[[Category: Spraggon G]]
-[[Category: Schultz, P G.]]
+[[Category: Turner JM]]
-[[Category: Spraggon, G.]]
-[[Category: Turner, J M.]]
-[[Category: Ketone]]
-[[Category: Structural plasticity]]
-[[Category: Trna synthetase]]
-[[Category: Unnatural amino acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:37:07 2008''