Pathak_1988_J.Mol.Biol_204_435

Reference

Title : X-ray crystallographic structure of dienelactone hydrolase at 2.8 A - Pathak_1988_J.Mol.Biol_204_435
Author(s) : Pathak D , Ngai KL , Ollis D
Ref : Journal of Molecular Biology , 204 :435 , 1988
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.

PubMedSearch : Pathak_1988_J.Mol.Biol_204_435
PubMedID: 3221394
Gene_locus related to this paper: psepu-clcd1

Related information

Substrate Dienelactone
Gene_locus psepu-clcd1
Family Dienelactone_hydrolase
Structure 1DIN

Citations formats

Pathak D, Ngai KL, Ollis D (1988)
X-ray crystallographic structure of dienelactone hydrolase at 2.8 A
Journal of Molecular Biology 204 :435

Pathak D, Ngai KL, Ollis D (1988)
Journal of Molecular Biology 204 :435