Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4 A resolution.
The crystal structure of an alkaline protease from Bacillus alcalophilus has been determined by X-ray diffraction at 2.4 A resolution. The enzyme crystallizes in space group P2(1)2(1)2(1) with lattice constants a = 53.7, b = 61.6, c = 75.9 A. The structure was solved by molecular replacement using the structure of subtilisin Carlsberg as search model. Refinement using molecular dynamics and restrained least squares methods results in a crystallographic R-factor of 0.185. The tertiary structure is very similar to that of subtilisin Carlsberg. The greatest structural differences occur in loops at the surface of the protein.
Sobek
H
H
Gesellschaft für Biotechnologische Forschung, Braunschweig, FRG.
Hecht
H J
HJ
Hofmann
B
B
Aehle
W
W
Schomburg
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D
D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D008958:Models, Molecular; D011487:Protein Conformation; D012984:Software; D013381:Subtilisins / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D013381:Subtilisins