title: Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.
abstract: 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.
authors: SIPBS, University of Strathclyde, 27 Taylor Street, Glasgow, Scotland, UK.
authors: Michael
authors: M
authors: Fairhead
authors: Kenneth A
authors: KA
authors: Johnson
authors: Thomas
authors: T
authors: Kowatz
authors: Stephen A
authors: SA
authors: McMahon
authors: Lester G
authors: LG
authors: Carter
authors: Muse
authors: M
authors: Oke
authors: Huanting
authors: H
authors: Liu
authors: James H
authors: JH
authors: Naismith
authors: Christopher F
authors: CF
authors: van der Walle
mesh_terms: D056668:Cathepsin L; D002403:Cathepsins / Q000737:chemistry*; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
chemical_list: D011993:Recombinant Fusion Proteins; C112571:silicatein alpha; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056668:Cathepsin L