期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 33, 页码 9687-9690出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201504014
关键词
groupII introns; NMR spectroscopy; ribozymes; RNA; structure-function relationships
资金
- Swiss National Science Foundation
- FP7 Marie Curie Intra European Fellowship
- University of Zurich
NMR spectroscopy has revealed pH-dependent structural changes in the highly conserved catalytic domain5 of a bacterial groupII intron. Two adenines with pK(a)values close to neutral pH were identified in the catalytic triad and the bulge. Protonation of the adenine opposite to the catalytic triad is stabilized within a G(syn)-AH(+)(anti) base pair. The pH-dependent anti-to-syn flipping of this G in the catalytic triad modulates the known interaction with the linker region between domains2 and 3 (J23) and simultaneously the binding of the catalytic Mg2+ ion to its backbone. Hence, this here identified shifted pK(a)value controls the conformational change between the two steps of splicing.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据