Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase.
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.[1]References
- Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase. Liao, D.I., Remington, S.J. J. Biol. Chem. (1990) [Pubmed]
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