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• W2085985889 abstract "Although site-bound Mg2+ ions have been proposed to influence RNA structure and function, establishing the molecular properties of such sites has been challenging due largely to the unique electrostatic properties of the RNA biopolymer. We have previously determined that, in solution, the hammerhead ribozyme (a self-cleaving RNA) has a high-affinity metal ion binding site characterized by a Kd,app < 10 μM for Mn2+ in 1 M NaCl and speculated that this site has functional importance in the ribozyme cleavage reaction. Here we determine both the precise location and the hydration level of Mn2+ in this site using ESEEM (electron spin−echo envelope modulation) spectroscopy. Definitive assignment of the high-affinity site to the activity-sensitive A9/G10.1 region is achieved by site-specific labeling of G10.1 with 15N guanine. The coordinated metal ion retains four water ligands as measured by 2H ESEEM spectroscopy. The results presented here show that a functionally important, specific metal binding site is uniquely populated in the hammerhead ribozyme even in a background of high ionic strength. Although it has a relatively high thermodynamic affinity, this ion remains partially hydrated and is chelated to the RNA by just two ligands." @default.
• W2085985889 created "2016-06-24" @default.
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• W2085985889 date "2006-12-01" @default.
• W2085985889 modified "2023-10-07" @default.
• W2085985889 title "Coordination Environment of a Site-Bound Metal Ion in the Hammerhead Ribozyme Determined by ¹⁵N and ²H ESEEM Spectroscopy" @default.
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• W2085985889 doi "https://doi.org/10.1021/ja057035p" @default.
• W2085985889 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3217337" @default.
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