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J. Biol. Chem., Vol. 265, Issue 12, 6528-6531, Apr, 1990

Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase

DI Liao and SJ Remington
Institute of Molecular Biology, University of Oregon, Eugene 97403.

The structure of serine carboxypeptidase II from wheat bran has been determined to 3.5-A resolution by multiple isomorphous replacement, solvent flattening, and crystallographic refinement. The amino acid sequence has been fit to the electron density map and the model refined to a conventional crystallographic R factor of 20.9%. The molecule is an alpha + beta protein and contains a "catalytic triad" (Asp338, His397, and Ser146) similar in arrangement to those in chymotrypsin and subtilisin. The -fold of the polypeptide backbone is, however, completely different from those enzymes. This suggests that this is a third example of convergent evolution to a common enzymatic mechanism. The -fold is, on the other hand, surprisingly similar to that of the zinc proteinase carboxypeptidase A.
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