Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin.
Thermitase, the thermostable alkaline protease from Thermoactinomyces vulgaris, has been crystallised in a 1:1 complex with eglin, the inhibitor from the medical leech. Two large crystals were grown, with cell dimensions of a = 49.3 A, b = 67.3 A, c = 90.5 A and space group P2(1)2(1)2(1). The crystals are relatively tightly packed with Vm = 2.1 A3/Da. Three-dimensional data to 1.9 A have been recorded from one of these crystals. The orientation and position of the complex in the unit cell have been established using the subtilisin Carlsberg-eglin structure as a model. The structure of the complex is being refined by restrained least-squares. The present crystallographic R factor (= sigma parallel Fo - Fc parallel/sigma/Fo parallel) is 26% at 2.5 A resolution.
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D010450:Endopeptidases; D007865:Leeches; D008848:Micromonosporaceae / Q000201:enzymology*; D008969:Molecular Sequence Data; D011506:Proteins; D012697:Serine Endopeptidases; D015843:Serpins
D011506:Proteins; D015843:Serpins; C028656:eglin proteinase inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase