Abstract
Original language | English |
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Pages (from-to) | 739-744 |
Number of pages | 6 |
Journal | Nature Chemical Biology |
Volume | 10 |
Issue number | 9 |
DOIs | |
Publication status | Published - Sep 2014 |
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Crystal structure and mechanistic investigation of the twister ribozyme. / Liu, Yijin; Wilson, Timothy J.; McPhee, Scott A.; Lilley, David M. J. (Lead / Corresponding author).
In: Nature Chemical Biology, Vol. 10, No. 9, 09.2014, p. 739-744.Research output: Contribution to journal › Article
TY - JOUR
T1 - Crystal structure and mechanistic investigation of the twister ribozyme
AU - Liu, Yijin
AU - Wilson, Timothy J.
AU - McPhee, Scott A.
AU - Lilley, David M. J.
PY - 2014/9
Y1 - 2014/9
N2 - We present a crystal structure at 2.3-Å resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.
AB - We present a crystal structure at 2.3-Å resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.
U2 - 10.1038/nchembio.1587
DO - 10.1038/nchembio.1587
M3 - Article
C2 - 25038788
VL - 10
SP - 739
EP - 744
JO - Nature Chemical Biology
JF - Nature Chemical Biology
SN - 1552-4450
IS - 9
ER -