Ionic interactions and the global conformations of the hammerhead ribozyme

Bassi, Gurminder S; Møllegard, Niels-Erik; Murchie, Alastair I. H.; Von Kitzing, Eberhard; Lilley, David M. J.

doi:10.1038/nsb0195-45

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Ionic interactions and the global conformations of the hammerhead ribozyme

MPS-Authors

/persons/resource/persons95816

Von Kitzing, Eberhard
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://www.nature.com/nsmb/journal/v2/n1/pdf/nsb0195-45.pdf
(Any fulltext)

https://dx.doi.org/10.1038/nsb0195-45
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Bassi, G. S., Møllegard, N.-E., Murchie, A. I. H., Von Kitzing, E., & Lilley, D. M. J. (1995). Ionic interactions and the global conformations of the hammerhead ribozyme. Nature Structural and Molecular Biology, 2(1), 45-55. doi:10.1038/nsb0195-45.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-54DC-C

Abstract

Here we investigate the global conformation of the hammerhead ribozyme. Electrophoretic studies demonstrate that the structure is folded in response to the concentration and type of ions present. Folding based on colinear alignment of arms II and III is suggested, with a variable angle subtended by the remaining helix I. In the probable active conformation, a small angle is subtended between helices I and II. Using uranyl photocleavage, an ion binding site has been detected in the long single-stranded region. The folded conformation could generate a preactivation of the scissile bond to permit in-line attack of the 2'-hydroxyl group, with a bound metal ion playing an integral role in the chemistry.