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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2020.1
- 수록면
- 350 - 359 (10page)
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이 논문의 연구 히스토리 (2)
2020
Structural studies of eukaryotic aminoacyl-tRNA synthetases: Fungal Isoleucyl-tRNA synthetase and Metazoan Glutamyl- and Isoleucyl-tRNA synthetase complex
정시성
생명과학과
2020.01
학위논문
Structural Basis for the Antibiotic Resistance of Eukaryotic Isoleucyl-tRNA Synthetase
정시성
,
김설희
,
Sung Ho Ryu
외 2명
Molecules and Cells
2020.01
학술저널
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Pathogenic aminoacyl-tRNA synthetases (ARSs) are attractive targets for anti-infective agents because their catalytic active sites are different from those of human ARSs. Mupirocin is a topical antibiotic that specifically inhibits bacterial isoleucyl-tRNA synthetase (IleRS), resulting in a block to protein synthesis. Previous studies on Thermus thermophilus IleRS indicated that mupirocin-resistance of eukaryotic IleRS is primarily due to differences in two amino acids, His581 and Leu583, in the active site. However, without a eukaryotic IleRS structure, the structural basis for mupirocin-resistance of eukaryotic IleRS remains elusive. Herein, we determined the crystal structure of Candida albicans IleRS complexed with Ile-AMP at 2.9 Å resolution. The largest difference between eukaryotic and prokaryotic IleRS enzymes is closure of the active site pocket by Phe55 in the HIGH loop; Arg410 in the CP core loop; and the second Lys in the KMSKR loop. The Ile-AMP product is lodged in a closed active site, which may restrict its release and thereby enhance catalytic efficiency. The compact active site also prevents the optimal positioning of the 9-hydroxynonanoic acid of mupirocin and plays a critical role in resistance of eukaryotic IleRS to anti-infective agents.
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참고문헌 (27)
참고문헌 신청
Adams, P. D. / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr. D. Biol. Crystallogr 66:213~221
Antonellis, A. / 2008 / The role of aminoacyl-tRNA synthetases in genetic diseases / Annu. Rev. Genomics Hum. Genet 9:87~107
Brown, J. R. / 1995 / Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications / Proc. Natl. Acad. Sci. U. S. A 92:2441~2445
Chen, V. B. / 2010 / MolProbity : all-atom structure validation for macromolecular crystallography / Acta Crystallogr. D. Biol. Crystallogr 66:12~21
Cusack, S. / 2000 / The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue / EMBO J 19:2351~2361
Antonellis, A. / 2008 / The role of aminoacyl-tRNA synthetases in genetic diseases / Annu. Rev. Genomics Hum. Genet 9:87~107
Brown, J. R. / 1995 / Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications / Proc. Natl. Acad. Sci. U. S. A 92:2441~2445
Chen, V. B. / 2010 / MolProbity : all-atom structure validation for macromolecular crystallography / Acta Crystallogr. D. Biol. Crystallogr 66:12~21
Cusack, S. / 2000 / The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue / EMBO J 19:2351~2361
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