Title : Three-dimensional structure of proteinase K at 0.15-nm resolution.

Pub. Date : 1988 Dec 1

PMID : 3203685






2 Functional Relationships(s)
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Protein Name
Organism
1 Besides this Cys72, proteinase K has two disulfide bonds, Cys34--Cys123 and Cys178--Cys249, which contribute to the stability of the tertiary structure consisting of an extended central parallel beta-sheet decorated by six alpha-helices, three short antiparallel beta-sheets, 18 beta-turns and involving several internal, structurally important water molecules. Water endogenous retrovirus group K member 7 Homo sapiens
2 Based on these experiments, a reaction mechanism is proposed where the peptide substrate forms a three-stranded antiparallel pleated sheet with the recognition site of proteinase K consisting of Ser132--Leu133--Gly134 on one side and Gly100--Ser101 on the other, followed by expulsion of the oxyanion hole water W335 and hydrolytic cleavage by the Asp39--His69--Serr224 triad. Water endogenous retrovirus group K member 7 Homo sapiens