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THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-CTHE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C
Structural highlights
Function[SUBT_BACPU] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [ICIC_HIRME] Inhibits both elastase and cathepsin G. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. See AlsoReferences |
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