Structural highlights
Function
[PRTB_STRGR] Has a primary specificity for large aliphatic or aromatic amino acids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the complex between the serine protease Streptomyces griseus protease B (SGPB) and the third domain of the Kazal-type ovomucoid inhibitor from turkey has been solved at 1.8-A resolution and refined to a conventional R factor of 0.125. As others have reported previously for analogous complexes of proteases and protein inhibitors, the inhibitor binds in a fashion similar to that of a substrate; it is not cleaved, but there is a close approach (2.7 A) of the active site nucleophile Ser-195 O gamma to the carbonyl carbon of the reactive peptide bond of the inhibitor. Contrary to the structural reports regarding the other enzyme-inhibitor complexes, we conclude that there is no evidence for a significant distortion of this peptide bond from planarity. The mechanism of inhibition can be understood in terms of the equilibrium thermodynamic parameters Ka, the enzyme-inhibitor association constant, and Khyd, the equilibrium constant for inhibitor hydrolysis. These thermodynamic parameters can be rationalized in terms of the observed structure.
Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.,Read RJ, Fujinaga M, Sielecki AR, James MN Biochemistry. 1983 Sep 13;22(19):4420-33. PMID:6414511[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Read RJ, Fujinaga M, Sielecki AR, James MN. Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution. Biochemistry. 1983 Sep 13;22(19):4420-33. PMID:6414511
