Crystal structure of the high-alkaline serine protease PB92 from Bacillus alcalophilus |
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Authors: | van der Laan JM; Teplyakov AV; Kelders H; Kalk KH; Misset O; Mulleners LJSM; Dijkstra BW |
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Affiliation: | Royal Gist-brocades NV, Research and Development PO Box 1, 2600 MA Delft
1BIOSON Research Institute, University of Groningen Nijenborgh 4, 9747 AG Groningen, The Netherlands |
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Abstract: | The crystal structure of a serine protease from the alkalophilicstrain Bacillus alcalophilus PB92 has been determined by X-raydiffraction at 1.75 Â resolution. The structure has beensolved by molecular replacement using the atomic model of subtilisinCarlsberg. The model of the PB92 protease has been refined toan R-factor of 14.0% and contains 1882 protein atoms, two calciumions and 188 water molecules. The overall folding of the polypeptide chain closely resembles that of the subtilisins. Furthermore,almost all of the secondary structure elements found in subtilisinCarlsberg are also present in the PB92 protease. The major differencesbetween the two structures are located around the deletion regions(residues 37 and 158161 in subtilisin Carlsberg) andin two loops which are known to be the most variable parts ofsubtilisin structures. Flexibility of one of these loops (residues126130 in the PB92 protease) is believed to account forthe inducedfit mechanism of substrate binding. |
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Keywords: | alkaline protease/ Bacillus alcalophilus/ serine protease/ X-ray structure |
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