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. 1984 Jun;3(6):1311–1314. doi: 10.1002/j.1460-2075.1984.tb01968.x

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

A Pähler, A Banerjee, J K Dattagupta, T Fujiwara, K Lindner, G P Pal, D Suck, G Weber, W Saenger
PMCID: PMC557514  PMID: 6378621

Abstract

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.

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Selected References

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