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          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents



ID: 22449.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
Ionic interactions and the global conformations of the hammerhead ribozyme
Translation of Title:Ionic interactions and the global conformations of the hammerhead ribozyme
Authors:Bassi, G. S.; Møllegaard, N.-E.; Murchie, A. I. H.; von Kitzing, Eberhard; Lilley, D. M. J.
Language:English
Date of Publication (YYYY-MM-DD):1995
Title of Journal:Nature Structural Biology
Journal Abbrev.:Nat. Struct. Biol.
Volume:2
Issue / Number:1
Start Page:45
End Page:55
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Zellphysiologie/
Identifiers:URI:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [Abstract]
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