Crystal Structure of Apo‐ and Metalated Thiolate containing RNase S as Structural Basis for the Design of Artificial Metalloenzymes by Peptide‐Protein Complementation12. Issue 14 (22nd October 2013)

• Record Type: Journal Article
• Authors: Genz, Maika; Singer, David; Hey‐Hawkins, Evamarie; Hoffmann, Ralf; Sträter, Norbert
• Is Part Of: Zeitschrift für anorganische und allgemeine Chemie. Volume 639:Issue 14(2013)
• Page Start: 2395
• Page End: 2400
• Publication Date: 2013-10-22
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry -- Periodicals; 540
• DOI: 10.1002/zaac.201300410
• Languages: English
• ISSNs: 0044-2313

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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 Hg^II 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.</p> </abstract>