1esb: Difference between revisions

Revision as of 01:48, 1 July 2008

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File:1esb.png

Template:STRUCTURE 1esb

DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASEDIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE

Template:ABSTRACT PUBMED 8049229

About this StructureAbout this Structure

1ESB is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

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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+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8049229}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8049229}}
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 [[Category: Rasmussen, B.]]
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