COLD-ADAPTION OF ENZYMES: STRUCTURAL COMPARISON BETWEEN SALMON AND BOVINE TRYPSINS

Cold adaption of enzymes: structural comparison between salmon and bovine trypsins.

Crystallization and Preliminary X-Ray Crystallographic Studies of Benzamidine-Inhibited Trypsin from the North Atlantic Salmon (Salmo Salar)

The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors

THE CALCIUM IS ION IS BOUND IN A MANNER SIMILAR TO THAT OBSERVED IN BOVINE TRYPSIN.
THE AMINO ACID NUMBERING SCHEME USED IS ADOPTED FROM CHYMOTRYPSINOGEN.

THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT METHODS,
USING THE MERLOT-PACKAGE (FITZGERALD, P. (1988) J.APPL.
CRYST., 21, 273-278), AND THE REFINED MODEL OF
BOVINE TRYPSIN AS SEARCH MODEL (PROTEIN DATA BANK, ENTRY
3PTB).

THIS ENTRY WAS REFINED USING A NON-STANDARD SETTING FOR
THE SPACE GROUP P 21 21 2. THE FOLLOWING SYMMETRY
OPERATORS MUST BE USED TO GENERATE CRYSTALLOGRAPHICALLY
RELATED MOLECULES.
X, Y, Z
-X, 1/2+Y, -Z
1/2+X, -Y, -Z
1/2-X, 1/2-Y, Z

TRYPSIN (E.C.3.4.21.4) COMPLEXED WITH BENZAMIDINE INHIBITOR