1qe0: Difference between revisions
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==CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE== | ==CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE== | ||
<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QE0 FirstGlance]. <br> | <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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QE0 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qe/1qe0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qe/1qe0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1qe0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1qe0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Histidine--tRNA ligase]] | [[Category: Histidine--tRNA ligase]] | ||
[[Category: Large Structures]] | |||
[[Category: Abdel-Meguid, S S]] | [[Category: Abdel-Meguid, S S]] | ||
[[Category: Blackburn, M N]] | [[Category: Blackburn, M N]] | ||
Revision as of 10:20, 7 August 2019
CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASECRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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