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X-ray crystal structures of staphyllococcal nuclease complexed with the competitive inhibitor cobalt and nucleotide
Journal article   Peer reviewed

X-ray crystal structures of staphyllococcal nuclease complexed with the competitive inhibitor cobalt and nucleotide

Patrick J Loll, Stephen Quirk, Eaton E Lattman and R. Michael Garavito
Biochemistry (Easton), Vol.34(13), p4316
04 Apr 1995

Abstract

Analysis Cobalt Nucleases Nucleotides Staphylococcus Usage
The ternary complexes of staphyllococcal nuclease with cobalt(II) and the mononucleotide possess different conformations in their metal-binding sites. In the first cobalt complex the cobalt ion is displaced 1.94 degree Angstroms from the common calcium position and the active site is possessed by a salt bridge between Asp-21 and Lys-70. The cobalt ion in the second structure binds with 0.36 degree Angstrom from the calcium position.

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