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Molecular Dynamics Simulation Study for Pre- and Post-transfer Substrate Binding of ValRS Editing Reaction

등록일
2008년 2월 14일 11시 10분 29초
접수번호
1291
발표코드
31P59포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
Bharatham Nagakumar, Bharatham Kavitha, 이근우1
경상대학교 응용생명과학부,
1경상대학교 생화학과 응용생명과학부 EB-NCRC,
Aminoacyl-tRNA synthetases (AARSs) are unexploited anti-bacterial targets which are essential enzymes involved in protein biosynthesis. The accuracy of protein synthesis depends on the specific recognition of amino acids and tRNAs by AARSs. Valyl-tRNA synthetase (ValRS) should discriminate the cognate valine from the non-cognate, isosteric threonine, which has a quite similar shape and size as valine. To maintain high translational fidelity, these AARSs catalyze proof-reading (editing) reactions in which the mis-products are hydrolyzed. In this study we have used Gromacs 3.3.1 software and Amber99 forcefield for 5 or 2ns MD simulations. Based on our results we propose that Thr-AMP or Thr-A76 binds strongly at editing site which can be hydrolyzed further when compared to Val-AMP or Val-A76 respectively. Our results support the possibility, for the existence of pre-transfer mechanism in valyl-tRNA synthetase.

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