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[[Image:1li7.gif|left|200px]]
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{{STRUCTURE_1li7|  PDB=1li7  |  SCENE=  }}
'''Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound'''


==Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound==
<StructureSection load='1li7' size='340' side='right'caption='[[1li7]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1li7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LI7 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <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=1li7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li7 OCA], [https://pdbe.org/1li7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1li7 RCSB], [https://www.ebi.ac.uk/pdbsum/1li7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1li7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYC_ECOLI SYC_ECOLI]
== 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/li/1li7_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=1li7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cysteinyl-tRNA synthetase (CysRS) is highly specific for synthesis of cysteinyl adenylate, yet does not possess the amino acid editing activity characteristic of many other tRNA synthetases. To elucidate how CysRS is able to distinguish cysteine from non-cognate amino acids, crystal structures of the Escherichia coli enzyme were determined in apo and cysteine-bound states. The structures reveal that the substrate cysteine thiolate forms a single direct interaction with a zinc ion bound at the base of the active site cleft, in a trigonal bipyramidal geometry together with four highly conserved protein side chains. Cysteine binding induces movement of the zinc ion towards substrate, as well as flipping of the conserved Trp205 indole ring to pack on the thiol side chain. The imidazole groups of five conserved histidines lie adjacent to the zinc ion, forming a unique arrangement suggestive of functional significance. Thus, amino acid discrimination without editing arises most directly from the favorable zinc-thiolate interaction, which is not possible for non-cognate substrates. Additional selectivity may be generated during the induced-fit conformational changes that help assemble the active site.


==Overview==
Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase.,Newberry KJ, Hou YM, Perona JJ EMBO J. 2002 Jun 3;21(11):2778-87. PMID:12032090<ref>PMID:12032090</ref>
Cysteinyl-tRNA synthetase (CysRS) is highly specific for synthesis of cysteinyl adenylate, yet does not possess the amino acid editing activity characteristic of many other tRNA synthetases. To elucidate how CysRS is able to distinguish cysteine from non-cognate amino acids, crystal structures of the Escherichia coli enzyme were determined in apo and cysteine-bound states. The structures reveal that the substrate cysteine thiolate forms a single direct interaction with a zinc ion bound at the base of the active site cleft, in a trigonal bipyramidal geometry together with four highly conserved protein side chains. Cysteine binding induces movement of the zinc ion towards substrate, as well as flipping of the conserved Trp205 indole ring to pack on the thiol side chain. The imidazole groups of five conserved histidines lie adjacent to the zinc ion, forming a unique arrangement suggestive of functional significance. Thus, amino acid discrimination without editing arises most directly from the favorable zinc-thiolate interaction, which is not possible for non-cognate substrates. Additional selectivity may be generated during the induced-fit conformational changes that help assemble the active site.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1LI7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI7 OCA].
</div>
<div class="pdbe-citations 1li7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase., Newberry KJ, Hou YM, Perona JJ, EMBO J. 2002 Jun 3;21(11):2778-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032090 12032090]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
[[Category: Cysteine--tRNA ligase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hou, Y M.]]
[[Category: Hou Y-M]]
[[Category: Newberry, K J.]]
[[Category: Newberry KJ]]
[[Category: Perona, J J.]]
[[Category: Perona JJ]]
[[Category: Cysteine]]
[[Category: E coli]]
[[Category: Trna synthetase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:56:50 2008''

Latest revision as of 09:14, 16 August 2023

Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound

1li7, resolution 2.60Å

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