1qe0
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1qe0' size='340' side='right'caption='[[1qe0]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1qe0' size='340' side='right'caption='[[1qe0]], [[Resolution|resolution]] 2.70Å' 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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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]] | ||
| Line 17: | Line 19: | ||
</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®/PubMed®, 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 | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Blackburn | + | [[Category: Abdel-Meguid SS]] |
| - | [[Category: Chohan | + | [[Category: Blackburn MN]] |
| - | [[Category: Hibbs | + | [[Category: Chohan IK]] |
| - | [[Category: Janson | + | [[Category: Hibbs M]] |
| - | [[Category: Qiu | + | [[Category: Janson CA]] |
| - | + | [[Category: Qiu X]] | |
| - | + | ||
| - | + | ||
Revision as of 06:03, 17 April 2024
CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE
| |||||||||||
