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  • 03월 04일 13시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Crystal Structure Alanysis of Nuclear Thiol Peroxidase

등록일
2005년 2월 17일 13시 56분 17초
접수번호
0891
발표코드
23P181포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
최정원, 신환철1
수원대학교 화학과,
1서울대학교 화학과,
Yeast nucleus-localized thiol peroxidase(nTPx) is a functional peroxidase with two cysteine residues. For the structural analysis of reduced conformation of this protein, two cysteine residues were mutated by serine. The nTPx-mutant protein is crystallized by sparse matrix crystal screening using hanging drop method. Initial crystal has a rare hairy looking thin needle-like morphology. A series of optimization process was undertaken by a systematic approach. The crystal quality has been improved by adding heavy atoms such as Hg and Ni, and it has been found out that the different metal cations result in different crystal forms. The crystal structure has been solved by molecular replacement method since the sequence of this protein is homologous with the AhpC peroxiredoxin family. Compared with other peroxiredoxin structures, this enzyme should have a typical 2-Cys redox mechanism.

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