Crystal structure and silica condensing activities of silicatein α–cathepsin L chimeras

• DOI: 10.1039/b718264c
• Publication Date: 2008-02-21T14:30:47Z
• Authors: Michael Fairhead; Kenneth A. Johnson; Thomas Kowatz; Stephen A. McMahon; Lester G. Carter; Muse Oke; Huanting Liu; James H. Naismith; Christopher F. va...
• Keywords: Models, Molecular; 0301 basic medicine; Cysteine Endopeptidases; 03 medical and health sciences; Pharmacy and materia medica; Protein Conformation; Cathepsin L; Recombinant Fusion Proteins; Therapeutics. Pharmacology; 540; Microbiology; Cathepsins

Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 A crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation.