The sequence and X-ray structure of the trypsin from Fusarium oxysporum
- 1 June 1993
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 6 (4) , 341-348
- https://doi.org/10.1093/protein/6.4.341
Abstract
The trypsin from Fusarium oxysporum is equally homologous to trypsins from Streptomyces griseus, Streptomyces erythraeus and to bovine trypsin. A DFP (diisopropylfluorophosphate) inhibited form of the enzyme has been crystallized from 1.4 M Na2SO4, buffered with citrate at pH 5.0–5.5. The crystals belong to space group P21 with cell parameters a=33.43 Å, b=67.65 Å, c=39.85 Å and β=107.6°. There is one protein molecule in the asymmetric unit. X-ray diffraction data to a resolution of 1.8 Å were collected on film using synchrotron radiation. The structure was solved by molecular replacement using models of bovine and S.griseus trypsins and refined to an R-factor of 0.141. The overall fold is similar to other trypsins, with some insertions and deletions. There is no evidence of the divalent cation binding sites seen in other trypsins. The covalently bound inhibitor molecule is clearly visible.Keywords
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