1QE0

CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE

Summary for 1QE0

• Entry DOI: 10.2210/pdb1qe0/pdb
• Descriptor: Histidine--tRNA ligase (2 entities in total)
• Functional Keywords: class ii trna synthetase, beta sheet, ligase
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm : P60911
• Total number of polymer chains: 2
• Total formula weight: 96669.50

Authors

Qiu, X.,Janson, C.A.,Blackburn, M.N.,Chohan, I.K.,Hibbs, M.,Abdel-Meguid, S.S. (deposition date: 1999-07-12, release date: 2000-07-12, Last modification date: 2024-10-30)

Primary citation

Qiu, X.,Janson, C.A.,Blackburn, M.N.,Chhohan, I.K.,Hibbs, M.,Abdel-Meguid, S.S.
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases.
Biochemistry, 38:12296-12304, 1999

PubMed Abstract: 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.

PubMed: 10493797
DOI: 10.1021/bi990482v

Experimental method

X-RAY DIFFRACTION (2.7 Å)