1esa
From Proteopedia
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DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE
Overview
The method of X-ray crystallographic cryoenzymology has been used to determine the crystal structure of a kinetically significant species on the reaction pathway of a crystalline enzyme. The structure of a specific acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and refined against X-ray diffraction data at 2.3-A resolution. The difference Fourier electron density map clearly shows electron density for the trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was stabilized at -55 degrees C during data collection, taking advantage of the glass transition in protein dynamics that occurs at around -50 degrees C.
About this Structure
1ESA is a Single protein structure of sequence from Sus scrofa with and as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.
Reference
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase., Ding X, Rasmussen BF, Petsko GA, Ringe D, Biochemistry. 1994 Aug 9;33(31):9285-93. PMID:8049229
Page seeded by OCA on Thu Feb 21 12:31:01 2008
