1JIL

Crystal structure of S. aureus TyrRS in complex with SB284485

1JIL の概要

• エントリーDOI: 10.2210/pdb1jil/pdb
• 関連するPDBエントリー: 1JII 1JIJ 1JIK
• 分子名称: tyrosyl-tRNA synthetase, [2-AMINO-3-(4-HYDROXY-PHENYL)-PROPIONYLAMINO]- (3,4,5-TRIHYDROXY-6-METHYL-TETRAHYDRO-PYRAN-2-YL)- ACETIC ACID (3 entities in total)
• 機能のキーワード: tyrosyl-trna synthetase, staphylococcus aureus, truncation, structure based inhibitor design, ligase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48039.83

構造登録者

Qiu, X.,Janson, C.A.,Smith, W.W.,Jarvest, R.L. (登録日: 2001-07-02, 公開日: 2001-10-26, 最終更新日: 2023-08-16)

主引用文献

Qiu, X.,Janson, C.A.,Smith, W.W.,Green, S.M.,McDevitt, P.,Johanson, K.,Carter, P.,Hibbs, M.,Lewis, C.,Chalker, A.,Fosberry, A.,Lalonde, J.,Berge, J.,Brown, P.,Houge-Frydrych, C.S.,Jarvest, R.L.
Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.
Protein Sci., 10:2008-2016, 2001

PubMed Abstract: SB-219383 and its analogues are a class of potent and specific inhibitors of bacterial tyrosyl-tRNA synthetases. Crystal structures of these inhibitors have been solved in complex with the tyrosyl-tRNA synthetase from Staphylococcus aureus, the bacterium that is largely responsible for hospital-acquired infections. The full-length enzyme yielded crystals that diffracted to 2.8 A resolution, but a truncated version of the enzyme allowed the resolution to be extended to 2.2 A. These inhibitors not only occupy the known substrate binding sites in unique ways, but also reveal a butyl binding pocket. It was reported that the Bacillus stearothermophilus TyrRS T51P mutant has much increased catalytic activity. The S. aureus enzyme happens to have a proline at position 51. Therefore, our structures may contribute to the understanding of the catalytic mechanism and provide the structural basis for designing novel antimicrobial agents.

PubMed: 11567092
DOI: 10.1110/ps.18001

実験手法

X-RAY DIFFRACTION (2.2 Å)