Structure-guided studies of key base, sugar, and phosphate mutations in the twister-sister ribozyme, suggest contributions to the cleavage chemistry from interactions between a guanine at the active.
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From this effort, clear trends were established to generate a structure–activity relationship and determine requirements for binding. Substitution of an electron withdrawing trifluoromethyl group in.
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Coordinates, structure factors and chemical shift assignments have been deposited in the Protein Data Bank and the Biological Magnetic Resonance Data Bank under PDB accession codes 6GF1 and 6GF2 and.
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1 Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. 2 A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences.
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1 Institute of Neuropathology, University Hospital of Zürich, University of Zürich, 8091 Zürich, Switzerland. 2 Physical Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich,
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Figure 1: WRN-exo fold, structure and active site structural chemistry. Figure 2: WRN-exo metal-ion dependence and structural analyses. Figure 4: Nuclease activities of WRN, WRN-exo and WRN-exo point.
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We recently described the directed evolution of PON1 and PON3 variants that express in a soluble and active form in Escherichia coli and have enzymatic properties identical to those reported for PONs.
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