Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin

FEBS Letters

Dauter, Zbigniew¹  Betzel, Christian¹  Wilson, Keith S.¹  Höhne, Wolfgang-Ernst²  Ingelman, Margareta¹ 

[1] European Molecular Biology Laboratory, c/o DESY, Notkestrasse 85, D-2000 Hamburg 52, FRG;Institut für Biochemie, Humboldt-Universität Berlin, Hessische Strasse 3-4, DDR-1040 Berlin, GDR

关键词: Thermitase;    Serine proteinase;    Crystallography;    Thermostability;    Molecular replacement;    Ca2+ binding;   

DOI  :  10.1016/0014-5793(88)80309-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å, b = 67.3 Å, c = 90.5 Å and space group P2₁2₁2₁. The crystals are relatively tightly packed with V _m = 2.1 ų/Da. Three-dimensional data to 1.9 Å 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 (= Σ|F _o−F _c|/Σ|F _o) is 26% at 2.5 Å resolution.

【 授权许可】

Unknown