Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
Dauter
Z
Z
European Molecular Biology Laboratory (EMBL), Hamburg, Germany.
Betzel
C
C
Genov
N
N
Pipon
N
N
Wilson
K S
KS
D000595:Amino Acid Sequence; D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D007865:Leeches; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D011506:Proteins; D012697:Serine Endopeptidases / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D015843:Serpins; D013381:Subtilisins / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; C028656:eglin proteinase inhibitors; D012697:Serine Endopeptidases; D013381:Subtilisins; C021553:mesentericopeptidase