1qe0

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[[Image:1qe0.gif|left|200px]]
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{{Structure
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|PDB= 1qe0 |SIZE=350|CAPTION= <scene name='initialview01'>1qe0</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1qe0", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] </span>
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{{STRUCTURE_1qe0| PDB=1qe0 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qe0 OCA], [http://www.ebi.ac.uk/pdbsum/1qe0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qe0 RCSB]</span>
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'''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE'''
'''CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE'''
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[[Category: Janson, C A.]]
[[Category: Janson, C A.]]
[[Category: Qiu, X.]]
[[Category: Qiu, X.]]
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[[Category: beta sheet]]
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[[Category: Beta sheet]]
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[[Category: class ii trna synthetase]]
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[[Category: Class ii trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:10:27 2008''
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Revision as of 03:10, 3 May 2008

Image:1qe0.gif

Template:STRUCTURE 1qe0

CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE


Overview

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.

About this Structure

1QE0 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 06:10:27 2008

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