1jij: Difference between revisions

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New page: left|200px<br /><applet load="1jij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jij, resolution 3.2Å" /> '''Crystal structure of ...
 
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[[Image:1jij.jpg|left|200px]]<br /><applet load="1jij" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jij, resolution 3.2&Aring;" />
'''Crystal structure of S. aureus TyrRS in complex with SB-239629'''<br />


==Overview==
==Crystal structure of S. aureus TyrRS in complex with SB-239629==
SB-219383 and its analogues are a class of potent and specific inhibitors, of bacterial tyrosyl-tRNA synthetases. Crystal structures of these, inhibitors have been solved in complex with the tyrosyl-tRNA synthetase, from Staphylococcus aureus, the bacterium that is largely responsible for, hospital-acquired infections. The full-length enzyme yielded crystals that, diffracted to 2.8 A resolution, but a truncated version of the enzyme, allowed the resolution to be extended to 2.2 A. These inhibitors not only, occupy the known substrate binding sites in unique ways, but also reveal a, butyl binding pocket. It was reported that the Bacillus stearothermophilus, TyrRS T51P mutant has much increased catalytic activity. The S. aureus, enzyme happens to have a proline at position 51. Therefore, our structures, may contribute to the understanding of the catalytic mechanism and provide, the structural basis for designing novel antimicrobial agents.
<StructureSection load='1jij' size='340' side='right'caption='[[1jij]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jij]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JIJ 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=629:[2-AMINO-3-(4-HYDROXY-PHENYL)-PROPIONYLAMINO]-(1,3,4,5-TETRAHYDROXY-4-HYDROXYMETHYL-PIPERIDIN-2-YL)-+ACETIC+ACID'>629</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=1jij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jij OCA], [https://pdbe.org/1jij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jij RCSB], [https://www.ebi.ac.uk/pdbsum/1jij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jij ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYY_STAAE SYY_STAAE] 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).[HAMAP-Rule:MF_02006]
== 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/ji/1jij_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=1jij ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1JIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with 629 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JIJ OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors., Qiu X, Janson CA, Smith WW, Green SM, McDevitt P, Johanson K, Carter P, Hibbs M, Lewis C, Chalker A, Fosberry A, Lalonde J, Berge J, Brown P, Houge-Frydrych CS, Jarvest RL, Protein Sci. 2001 Oct;10(10):2008-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11567092 11567092]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Tyrosine--tRNA ligase]]
[[Category: Janson CA]]
[[Category: Janson, C.A.]]
[[Category: Jarvest RL]]
[[Category: Jarvest, R.L.]]
[[Category: Qiu X]]
[[Category: Qiu, X.]]
[[Category: Smith WW]]
[[Category: Smith, W.W.]]
[[Category: 629]]
[[Category: staphylococcus aureus]]
[[Category: structure based inhibitor design]]
[[Category: truncation]]
[[Category: tyrosyl-trna synthetase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:42:19 2007''

Latest revision as of 10:39, 7 February 2024

Crystal structure of S. aureus TyrRS in complex with SB-239629Crystal structure of S. aureus TyrRS in complex with SB-239629

Structural highlights

1jij is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYY_STAAE 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).[HAMAP-Rule:MF_02006]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1jij, resolution 3.20Å

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