1ile: Difference between revisions

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-[[Image:1ile.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1ile", 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.
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-{{STRUCTURE_1ile|  PDB=1ile  |  SCENE=  }}
-'''ISOLEUCYL-TRNA SYNTHETASE'''
+==ISOLEUCYL-TRNA SYNTHETASE==
+<StructureSection load='1ile' size='340' side='right'caption='[[1ile]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ile]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILE 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=ZN:ZINC+ION'>ZN</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=1ile FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ile OCA], [https://pdbe.org/1ile PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ile RCSB], [https://www.ebi.ac.uk/pdbsum/1ile PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ile ProSAT], [https://www.topsan.org/Proteins/RSGI/1ile TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYI_THET8 SYI_THET8] Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity).[HAMAP-Rule:MF_02003]
+== 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/il/1ile_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ile ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a "double-sieve" mechanism has already been proposed. The present crystal structures of the synthetase in complexes with L-isoleucine and L-valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular beta-barrel domain that protrudes from the aminoacylation domain.
-==Overview==
+Enzyme structure with two catalytic sites for double-sieve selection of substrate.,Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S Science. 1998 Apr 24;280(5363):578-82. PMID:9554847<ref>PMID:9554847</ref>
-High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a "double-sieve" mechanism has already been proposed. The present crystal structures of the synthetase in complexes with L-isoleucine and L-valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular beta-barrel domain that protrudes from the aminoacylation domain.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-ILE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILE OCA].
+</div>
+<div class="pdbe-citations 1ile" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Enzyme structure with two catalytic sites for double-sieve selection of substrate., Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S, Science. 1998 Apr 24;280(5363):578-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9554847 9554847]
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-[[Category: Single protein]]
+== References ==
-[[Category: Thermus thermophilus]]
+<references/>
-[[Category: Fukai, S.]]
+__TOC__
-[[Category: Konno, M.]]
+</StructureSection>
-[[Category: Nakama, T.]]
+[[Category: Large Structures]]
-[[Category: Nureki, O.]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+[[Category: Fukai S]]
-[[Category: Schimmel, P.]]
+[[Category: Konno M]]
-[[Category: Shimada, A.]]
+[[Category: Nakama T]]
-[[Category: Tateno, M.]]
+[[Category: Nureki O]]
-[[Category: Vassylyev, D G.]]
+[[Category: Schimmel P]]
-[[Category: Yokoyama, S.]]
+[[Category: Shimada A]]
-[[Category: Aminoacyl-trna synthetase]]
+[[Category: Tateno M]]
-[[Category: Riken structural genomics/proteomics initiative]]
+[[Category: Vassylyev DG]]
-[[Category: Rsgi]]
+[[Category: Yokoyama S]]
-[[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:07:28 2008''