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[[Image:1bbu.gif|left|200px]]
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{{STRUCTURE_1bbu|  PDB=1bbu  |  SCENE=  }}
'''LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE'''


==LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE==
<StructureSection load='1bbu' size='340' side='right'caption='[[1bbu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bbu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBU 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</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=1bbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbu OCA], [https://pdbe.org/1bbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbu RCSB], [https://www.ebi.ac.uk/pdbsum/1bbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYK1_ECOLI SYK1_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/bb/1bbu_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=1bbu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.


==Overview==
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding.,Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850<ref>PMID:11041850</ref>
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BBU 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=1BBU OCA].
</div>
<div class="pdbe-citations 1bbu" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding., Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P, Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11041850 11041850]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
[[Category: Escherichia coli]]
== References ==
[[Category: Lysine--tRNA ligase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Blanquet, S.]]
</StructureSection>
[[Category: Brevet, A.]]
[[Category: Escherichia coli K-12]]
[[Category: Brick, P.]]
[[Category: Large Structures]]
[[Category: Chen, J.]]
[[Category: Blanquet S]]
[[Category: Desogus, G.]]
[[Category: Brevet A]]
[[Category: Onesti, S.]]
[[Category: Brick P]]
[[Category: Plateau, P.]]
[[Category: Chen J]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Desogus G]]
[[Category: Ligase]]
[[Category: Onesti S]]
[[Category: Protein biosynthesis]]
[[Category: Plateau P]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:18:59 2008''

Latest revision as of 05:38, 9 August 2023

LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE

1bbu, resolution 2.70Å

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