Download MendeleyComplex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
Dauter, Z., Betzel, C., Genov, N., Pipon, N., Wilson, K.S.(1991) Acta Crystallogr B 47: 707-730
- PubMed: 1793542
- DOI: https://doi.org/10.1107/s0108768191004202
- Primary Citation of Related Structures:
1MEE - PubMed Abstract:
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.
Organizational Affiliation:
European Molecular Biology Laboratory (EMBL), Hamburg, Germany.
