scholarly journals A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class

2015 ◽  
Vol 54 (50) ◽  
pp. 15128-15133 ◽  
Author(s):  
Marija Košutić ◽  
Sandro Neuner ◽  
Aiming Ren ◽  
Sara Flür ◽  
Christoph Wunderlich ◽  
...  
Keyword(s):  
Phosphodiester Cleavage

scholarly journals Activity inhibition and crystal polymorphism induced by active-site metal swapping

2017 ◽  
Vol 73 (8) ◽  
pp. 641-649 ◽  
Author(s):  
Elsie Yekwa ◽  
Joelle Khourieh ◽  
Bruno Canard ◽  
Nicolas Papageorgiou ◽  
François Ferron
Keyword(s):  
Innate Immunity ◽  
Metal Ion ◽  
Inhibition Mechanism ◽  
Binding Affinities ◽  
Crystal Polymorphism ◽  
Processing Enzymes ◽  
Exonuclease Domain ◽  
Divalent Metal Ion ◽  
Phosphodiester Cleavage ◽  
The Stability

TheArenaviridaefamily is one of the two RNA viral families that encode a 3′–5′ exonuclease in their genome. An exonuclease domain is found in theArenaviridaenucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg2+(or Mn2+) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca2+) inhibits this enzymatic activity, in spite of the fact that Mg2+and Ca2+present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of theMopeia virusexonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined.

A 1.9 Å Crystal Structure of the HDV Ribozyme Precleavage Suggests both Lewis Acid and General Acid Mechanisms Contribute to Phosphodiester Cleavage

Biochemistry ◽  
2010 ◽  
Vol 49 (31) ◽  
pp. 6508-6518 ◽  
Author(s):  
Jui-Hui Chen ◽  
Rieko Yajima ◽  
Durga M. Chadalavada ◽  
Elaine Chase ◽  
Philip C. Bevilacqua ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Lewis Acid ◽  
General Acid ◽  
Hdv Ribozyme ◽  
Phosphodiester Cleavage

Comparative nucleophilic reactivities in phosphodiester cleavage

2002 ◽  
Vol 43 (23) ◽  
pp. 4179-4182 ◽  
Author(s):  
Robert A Moss ◽  
Barbara A McKernan
Keyword(s):  
Phosphodiester Cleavage

A Pentacoordinate Oxorhenium(V) Metallochelate Elicits Antibody Catalysts for Phosphodiester Cleavage

1997 ◽  
Vol 119 (17) ◽  
pp. 4088-4089 ◽  
Author(s):  
David P. Weiner ◽  
Torsten Wiemann ◽  
Mary M. Wolfe ◽  
Paul Wentworth ◽  
Kim D. Janda
Keyword(s):  
Phosphodiester Cleavage
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