1qe0: Difference between revisions

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<StructureSection load='1qe0' size='340' side='right'caption='[[1qe0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1qe0' size='340' side='right'caption='[[1qe0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qe0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QE0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qe0]] is a 2 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=1QE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QE0 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] </span></td></tr>
</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=1qe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qe0 OCA], [https://pdbe.org/1qe0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qe0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qe0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qe0 ProSAT]</span></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=1qe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qe0 OCA], [https://pdbe.org/1qe0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qe0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qe0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qe0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYH_STAAU SYH_STAAU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1qe0 ConSurf].
</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=1qe0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined at 2.7 A resolution. Several important loops in the active site either become disordered or adopt very different conformations compared to their ligand-bound states. These include the histidine A motif (Arg257-Tyr262) that is essential for substrate recognition, a loop (Gly52-Lys62) that seems to control the communication between the histidine and ATP binding sites, the motif 2 loop (Glu114-Arg120) that binds ATP, and the insertion domain that is likely to bind tRNA. These ligand-induced structural changes are supported by fluorescence experiments, which also suggest highly cooperative dynamics. A dynamic and cooperative active site is most likely necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism for improving charging fidelity.
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases.,Qiu X, Janson CA, Blackburn MN, Chhohan IK, Hibbs M, Abdel-Meguid SS Biochemistry. 1999 Sep 21;38(38):12296-304. PMID:10493797<ref>PMID:10493797</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qe0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histidine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abdel-Meguid, S S]]
[[Category: Staphylococcus aureus]]
[[Category: Blackburn, M N]]
[[Category: Abdel-Meguid SS]]
[[Category: Chohan, I K]]
[[Category: Blackburn MN]]
[[Category: Hibbs, M]]
[[Category: Chohan IK]]
[[Category: Janson, C A]]
[[Category: Hibbs M]]
[[Category: Qiu, X]]
[[Category: Janson CA]]
[[Category: Beta sheet]]
[[Category: Qiu X]]
[[Category: Class ii trna synthetase]]
[[Category: Ligase]]

Revision as of 06:03, 17 April 2024

CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE

1qe0, resolution 2.70Å

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