Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes
- 31 December 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 3 (3) , 161-172
- https://doi.org/10.1093/protein/3.3.161
Abstract
We compare the three-dimensional structures of thermitase and of proteinase K determined by X-ray crystallography to a resolution of 1.4 and 1.48 Å respectively. Both enzymes are relatively stable towards heat and denaturating agents and are representative of a subgroup of subtilisins characterized by a free SH group close to the active site histidine. Even though they have low sequence homology, the overall tertiary structures are highly conserved. The high resolution structures are compared in terms of the overall fold of the molecules, the active sites, the calcium binding sites, disulphide bridge positions, the positions of the charged residues and the solvent structure. Most subtilisins such as thermitase are of prokaryotic origin and proteinase K is up to now the only known eukaryotic structure.This publication has 3 references indexed in Scilit:
- 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
- X‐ray and model‐building studies on the specificity of the active site of proteinase KProteins-Structure Function and Bioinformatics, 1988
- The high‐resolution X‐ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalisEuropean Journal of Biochemistry, 1987