1mee

Publication Abstract from PubMed

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.

Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.,Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:1793542^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.