Crystal structure of apo- and metalated thiolate containing RNase S as structural basis for the design of artificial metalloenzymes by peptide-protein complementation

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Abstract

Ribonuclease S (RNase S) is a versatile model system to introduce non-canonical amino acids into a protein scaffold by self-assembly of the protein complex from S-protein and S-peptide. We have introduced two cysteines into the S-peptide replacing lysine-7 and glutamine-11 of the α-helical region of this peptide. The crystal structure of this variant was determined in the apo state and in complex with HgII ions. These structures serve as a template for the construction of artificial hybrid catalysts based on RNase S, e.g. for phosphanyl amino acids complexing transition metal ions for organometallic catalysis. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Genz, M., Singer, D., Hey-Hawkins, E., Hoffmann, R., & Sträter, N. (2013). Crystal structure of apo- and metalated thiolate containing RNase S as structural basis for the design of artificial metalloenzymes by peptide-protein complementation. Zeitschrift Fur Anorganische Und Allgemeine Chemie, 639(14), 2395–2400. https://doi.org/10.1002/zaac.201300410

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