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• W2065202202 abstract "Reaction-intermediate analogs have been used to understand how phosphoryl transfer enzymes promote catalysis. Herein we report the first structure of a small ribozyme crystallized with a 3′-OH, 2′,5′-linkage in lieu of the normal phosphodiester substrate. The new structure shares features of the reaction coordinate exhibited in prior ribozyme structures including a vanadate complex that mimicked the oxyphosphorane transition state. As such, the structure exhibits reaction-intermediate traits that allow direct comparison of stabilizing interactions to the 3′-OH, 2′,5′-linkage contributed by the RNA enzyme and its protein counterpart, ribonuclease. Clear similarities are observed between the respective structures including hydrogen bonds to the non-bridging oxygens of the scissile phosphate. Other commonalities include carefully poised water molecules that may alleviate charge build-up in the transition state and placement of a positive charge near the leaving group. The advantages of 2′,5′-linkages to investigate phosphoryl-transfer reactions are discussed, and argue for their expanded use in structural studies." @default.
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• W2065202202 date "2008-06-01" @default.
• W2065202202 modified "2023-10-14" @default.
• W2065202202 title "Shared traits on the reaction coordinates of ribonuclease and an RNA enzyme" @default.
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• W2065202202 doi "https://doi.org/10.1016/j.bbrc.2008.04.036" @default.
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