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Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin.
Author(s) -
Pähler A.,
Banerjee A.,
Dattagupta J.K.,
Fujiwara T.,
Lindner K.,
Pal G.P.,
Suck D.,
Weber G.,
Saenger W.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01968.x
Subject(s) - information retrieval , combinatorics , mathematics , biology , computer science
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.