1qe0
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CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE
OverviewOverview
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 StructureAbout this Structure
1QE0 is a Single protein structure of sequence from Staphylococcus aureus. Active as Histidine--tRNA ligase, with EC number 6.1.1.21 Full crystallographic information is available from OCA.
ReferenceReference
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
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