| Autor: |
Fujinaga, M, Read, R J, Sielecki, A, Ardelt, W, Laskowski, M, James, M N |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; August 1982, Vol. 79 Issue: 16 p4868-4872, 5p |
| Abstrakt: |
We have determined the crystal structure of the molecular complex between Streptomyces griseus protease B (SGPB), a bacterial serine protease, and the third domain of the ovomucoid inhibitor from turkey. Restrained-parameter least-squares refinement of the structure with the 1.8-A intensity data set has resulted in an R factor of 0.125. The carbonyl carbon atom of the reactive bond between Leu-18 and Glu-19 in the inhibitor lies at a distance of 2.71 A from the O gamma atom of the nucleophilic Ser-195 in SGPB; this distance is 0.5 A shorter than a normal van der Waals contact. Unlike the reactive bond in the pancreatic trypsin inhibitor complexed with bovine trypsin, the Leu--Glu bond of the ovomucoid inhibitor is not distorted from planarity towards a pyramidal configuration. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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