1mee
THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C
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OverviewOverview
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.
About this StructureAbout this Structure
1MEE is a Protein complex structure of sequences from Bacillus pumilus and Hirudo medicinalis with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
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
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