Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease.

ABSTRACT: The main protease of the coronavirus causing severe acute respiratory syndrome performs proteolytic processing of the viral polyproteins. The active form of the enzyme is a homodimer with each subunit consisting of three structural domains. Domains I and II, hosting the complete catalytic machinery, constitute the N-terminal chymotrypsin-like folding scaffold and connect to the extra C-terminal domain III by a long loop. Previously, the domain III-truncated enzyme was demonstrated to fold independently into an intact chymotrypsin-like fold, but it showed no enzyme activity. To further delineate the structure-function relationships of the domain III and the long loop, we generated some truncated and mutated M(pro) forms bearing various combinations of the loop with other structural parts of

SUBMITTER: Tsai MY 

PROVIDER: S-EPMC7110190 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature