Refined Crystal Structure of the Molecular Complex of Streptomyces Griseus Protease B, a Serine Protease, with the Third Domain of the Ovomucoid Inhibitor from Turkey

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1982 Aug 1

PMID 6750612

Citations 12

Authors

M Fujinaga

R J Read

A Sielecki

W Ardelt

M Laskowski Jr

M N James

Affiliations

Soon will be listed here.

Abstract

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.

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