| Title : Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase - Liao_1990_J.Biol.Chem_265_6528 |
| Author(s) : Liao DI , Remington SJ |
| Ref : Journal of Biological Chemistry , 265 :6528 , 1990 |
| Abstract : 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. |
| ESTHER : Liao_1990_J.Biol.Chem_265_6528 |
| PubMedSearch : Liao_1990_J.Biol.Chem_265_6528 |
| PubMedID: 2324088 |
| Gene_locus related to this paper: wheat-cbp02 |
| Gene_locus related to this paper: wheat-cbp02 |
Liao DI, Remington SJ (1990)
Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase
Journal of Biological Chemistry
265 :6528
Liao DI, Remington SJ (1990)
Journal of Biological Chemistry
265 :6528