ChansonRolandV6, Main, Exploration, bibRecord, 000113

Protonation‐Dependent Base Flipping at Neutral pH in the Catalytic Triad of a Self‐Splicing Bacterial Group II Intron

Identifieur interne : 000113 ( Main/Exploration ); précédent : 000112; suivant : 000114

Protonation‐Dependent Base Flipping at Neutral pH in the Catalytic Triad of a Self‐Splicing Bacterial Group II Intron

Auteurs : Maria Pechlaner [Suisse] ; Daniela Donghi [Suisse] ; Veronika Zelenay [Suisse] ; Roland K. O. Sigel [Suisse]

Source :

Angewandte Chemie International Edition [ 1433-7851 ] ; 2015-08-10.

RBID : ISTEX:8C96F34B1AA4290803A13EAD1AB4C81CFE5FFDA9

English descriptors

Teeft :
- Amino proton, Avd5, Bacterial group, Base pair, Biol, Bulge, Bulge nucleotide, Bulge region, Catalytic, Catalytic triad, Chem, Chemical shift, Conformational change, Imino, Intron, Mismatch, Protonated, Protonation, Pyle, Secondary structure, Sigel, Solution structure, Strong interstrand, Structural change, Triad, Verlag gmbh, Weinheim angew.

Abstract

NMR spectroscopy has revealed pH‐dependent structural changes in the highly conserved catalytic domain 5 of a bacterial group II intron. Two adenines with pKa 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 domains 2 and 3 (J23) and simultaneously the binding of the catalytic Mg2+ ion to its backbone. Hence, this here identified shifted pKa value controls the conformational change between the two steps of splicing.

Strongly shifted: Two adenines in the highly conserved and catalytically essential domain 5 of group II introns become protonated near physiological pH values. The associated dynamic equilibria play an important role in group II intron assembly and catalysis.

Url:

https://api.istex.fr/ark:/67375/WNG-THLJBC6G-Z/fulltext.pdf

DOI: 10.1002/anie.201504014

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<front><div type="abstract" xml:lang="en">NMR spectroscopy has revealed pH‐dependent structural changes in the highly conserved catalytic domain 5 of a bacterial group II intron. Two adenines with pKa 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 domains 2 and 3 (J23) and simultaneously the binding of the catalytic Mg2+ ion to its backbone. Hence, this here identified shifted pKa value controls the conformational change between the two steps of splicing.</div>
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Protonation‐Dependent Base Flipping at Neutral pH in the Catalytic Triad of a Self‐Splicing Bacterial Group II Intron

Protonation‐Dependent Base Flipping at Neutral pH in the Catalytic Triad of a Self‐Splicing Bacterial Group II Intron

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri