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• W2066082196 abstract "T7 endonuclease I is a nuclease that is selective for the structure of the four-way DNA junction. The active site is similar to those of a number of restriction enzymes. We have solved the crystal structure of endonuclease I with a wild-type active site. Diffusion of manganese ions into the crystal revealed two peaks of electron density per active site, defining two metal ion-binding sites. Site 1 is fully occupied, and the manganese ion is coordinated by the carboxylate groups of Asp55 and Glu65, and the main chain carbonyl of Thr66. Site 2 is partially occupied, and the metal ion has a single protein ligand, the remaining carboxylate oxygen atom of Asp55. Isothermal titration calorimetry showed the sequential exothermic binding of two manganese ions in solution, with dissociation constants of 0.58 +/- 0.019 and 14 +/- 1.5 mM. These results are consistent with a two metal ion mechanism for the cleavage reaction, in which the hydrolytic water molecule is contained in the first coordination sphere of the site 1-bound metal ion." @default.
• W2066082196 created "2016-06-24" @default.
• W2066082196 creator A5081958301 @default.
• W2066082196 date "2002-07-01" @default.
• W2066082196 modified "2023-10-16" @default.
• W2066082196 title "Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I" @default.
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• W2066082196 doi "https://doi.org/10.1093/emboj/cdf337" @default.
• W2066082196 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/126086" @default.
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