1esb
From Proteopedia
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| , resolution 2.3Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1ESB is a Single protein structure of sequence from Sus scrofa. 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
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