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