1bbw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1bbw.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1bbw", 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_1bbw|  PDB=1bbw  |  SCENE=  }}
'''LYSYL-TRNA SYNTHETASE (LYSS)'''


==LYSYL-TRNA SYNTHETASE (LYSS)==
<StructureSection load='1bbw' size='340' side='right'caption='[[1bbw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bbw]] 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=1BBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBW 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbw OCA], [https://pdbe.org/1bbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbw RCSB], [https://www.ebi.ac.uk/pdbsum/1bbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbw 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/1bbw_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=1bbw 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>
1BBW 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=1BBW OCA].
</div>
<div class="pdbe-citations 1bbw" 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 11:19:03 2008''

Latest revision as of 05:38, 9 August 2023

LYSYL-TRNA SYNTHETASE (LYSS)

1bbw, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bbw&oldid=3819960"