X-ray crystallographic structure of dienelactone hydrolase at 2.8 A

Abstract

The structure of dienelactone hydrolase, an enzyme of the beta-ketoadipate pathway, has been determined at 2.8 A resolution using multiple isomorphous replacement techniques. An unambiguous assignment of C alpha atoms to electron density has been accomplished and a preliminary identification of the active site made. Dienelactone hydrolase is an alpha/beta protein consisting of an eight-stranded beta-pleated sheet with seven parallel strands, surrounded by seven helices. Preliminary enzyme inactivation data and an examination of the atomic model have implicated cysteine 123, histidine 202 and aspartate 171 with the active site of the enzyme. It is believed that the enzymic mechanism of dienelactone hydrolase may be similar to that of the thiol and serine proteases.