Autoprocessing mechanism of SARS-CoV 3CL protease

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3C like protease (3CLPro) of severe acute respiratory syndrome coronavirus (SARS-CoV) is synthesized as a part of polyprotein, and is excised by its own proteolytic activity. It has been previously reported that the precise processing of N-terminus of 3CLPro is required for efficient peptidase activity toward the florogenic peptide substrate. However, by the use of an E. coli in vitro protein synthesis system, we found that the C-terminal site of 3CLPro was efficiently cleaved even though N-terminal pro-sequence was not removed. Moreover, the substrate specificity of this autoprocessing activity was different from that of the mature enzyme. We also found the pocket for this special recognition by X-ray crystallography.