ChansonRolandV6, Main, Exploration, bibRecord, 000114

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

Identifieur interne : 000114 ( Main/Exploration ); précédent : 000113; suivant : 000115

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 [ 0044-8249 ] ; 2015-08-10.

RBID : ISTEX:4525170A759399EC8ABF8AB8E98845A3B86E23C4

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.

Stark verschoben: Zwei Adenine in der hoch konservierten und katalytisch essenziellen Domäne 5 von Gruppe‐II‐Introns werden bei physiologischen pH‐Werten protoniert. Die dazugehörigen dynamischen Gleichgewichte spielen bei der Assemblierung von Gruppe‐II‐Introns und ihren katalytischen Prozessen eine wichtige Rolle.

Url:

https://api.istex.fr/ark:/67375/WNG-LX0ZC4K3-L/fulltext.pdf

DOI: 10.1002/ange.201504014

Affiliations:

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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>
<div type="abstract" xml:lang="de">Stark verschoben: Zwei Adenine in der hoch konservierten und katalytisch essenziellen Domäne 5 von Gruppe‐II‐Introns werden bei physiologischen pH‐Werten protoniert. Die dazugehörigen dynamischen Gleichgewichte spielen bei der Assemblierung von Gruppe‐II‐Introns und ihren katalytischen Prozessen eine wichtige Rolle.</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)

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