A computational approach to the mechanism of self-cleavage of hammerhead RNA.
Author(s) -
H Y Mei,
Thomas W. Kaaret,
Thomas C. Bruice
Publication year - 1989
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.24.9727
Subject(s) - cleavage (geology) , chemistry , ribose , stereochemistry , crystallography , biochemistry , biology , paleontology , fracture (geology) , enzyme
Extensive minimization and dynamics computational studies of the hammerhead structural domain of the virusoid of lucerne transient streak virus have been carried out. The following observations at the self-cleavage position are derived from the resulting three-dimensional structure: (i) the cytosine base is at the surface and does not interact with another base (it is free to move), and (ii) the ribose-phosphate backbone is forced to take an abrupt turn since it bridges stems I and III, and this turn points the pro-S and pro-R oxygens of the phosphate to the inward side of the hammerhead. These structural features are independent of the hammerhead being open or closed and allow an unencumbered 3'- to 2'-endo conformational change of the ribose with the resultant creation of an unusual stereochemistry that allows a direct in-line self-cleavage reaction. In the closed hammerhead structure, interactions of stems I and II create a vacancy into which the catalytic hydrated Mg(II) may be docked on labile phosphate. This opening is not present if stems I and II are shortened.
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