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Three-dimensional structure of DNA sequence specificity subunit of type I restriction-modification enzyme

등록일
2005년 2월 17일 12시 06분 14초
접수번호
0848
발표코드
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발표시간
금 16시 : 30분
발표형식
심포지엄
발표분야
생명화학 - 생명Ⅰ: 신호전달과 분자 스위치
저자 및
공동저자
김정선, A.D.Giovanni1, J.Jancarik1, H.Yokota1, P.D.Adams1, R.Kim1, S.-H.Kim2
KRIBB,
1BSGC,
2Univ. of California, Berkeley,
Type I restriction enzymes are differentiated from type II and III enzymes by recognizing two specific DNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: an S-subunit, an M-subunit and an R-subunit. Crystal structure shows that two conserved regions in the middle and at the C-terminus form an alpha-helical coiled-coil structure. Two target recognition domains form globular structures with almost identical topologies and constitute two separate DNA binding clefts with a modeled DNA helix axis positioned across the CR helices. The structure suggests that the CRs act as a molecular ruler for the separation between two recognized DNA sequences and the relative orientation of the two DNA binding clefts distort the modeled dsDNA and expose target adenines from the recognized DNA sequences.

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