Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin

The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consi...

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Bibliographic Details
Published in:The EMBO journal 1984-06, Vol.3 (6), p.1311-1314
Main Authors: Pähler, A., Banerjee, A., Dattagupta, J.K., Fujiwara, T., Lindner, K., Pal, G.P., Suck, D., Weber, G., Saenger, W.
Format: Article
Language:English
Subjects:
bacteria
Bacteria - enzymology
crystal structure
Endopeptidase K
Endopeptidases - isolation & purification
Mitosporic Fungi - enzymology
Models, Molecular
Protein Conformation
serine proteinase
Structure-Activity Relationship
subtilisin
Subtilisins
Tritirachium album
X-Ray Diffraction
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Summary:The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consists of one monomer of 27 000 daltons mol. wt., approximately 50% higher than the so far assumed value of 18 500 daltons. The main chain fold of proteinase K shows a high degree of tertiary homology with the corresponding bacterial subtilisin BPN’. Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serine proteases in pro‐and eukaryotes.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1984.tb01968.x