Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin
- 15 August 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 236 (1) , 171-178
- https://doi.org/10.1016/0014-5793(88)80309-0
Abstract
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 Å3/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.Keywords
This publication has 19 references indexed in Scilit:
- Solvent content of protein crystalsPublished by Elsevier ,2006
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Synchrotron X-ray data collection and restrained least-squares refinement of the crystal structure of proteinase K at 1.5 Å resolutionActa crystallographica Section B, Structural science, crystal engineering and materials, 1988
- Amino acid sequence of proteinase K from the mold Tritirachium album LimberFEBS Letters, 1986
- Complete amino acid sequence of alkaline mesentericopeptidaseFEBS Letters, 1986
- Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin CarlsbergFEBS Letters, 1985
- Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin‐type proteinasesFEBS Letters, 1985
- Die Primärstruktur von Subtilisin DYHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- A new subfamily of microbial serine proteinases? Structural similarities of Bacillus thuringiensis and Thermoactinomyces vulgaris extracellular serine proteinasesBiochemical and Biophysical Research Communications, 1981
- Structure of Subtilisin BPN′ at 2.5 Å ResolutionNature, 1969