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4a3h

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(New page: 200px<br /> <applet load="4a3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="4a3h, resolution 1.65&Aring;" /> '''2',4' DINITROPHENYL...)
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Revision as of 19:39, 29 October 2007


4a3h, resolution 1.65Å

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2',4' DINITROPHENYL-2-DEOXY-2-FLURO-B-D-CELLOBIOSIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS AT 1.6 A RESOLUTION

Overview

The enzymatic hydrolysis of O-glycosidic linkages is one of the most, diverse and widespread reactions in nature and involves a classic, "textbook" enzyme mechanism. A multidisciplinary analysis of a, beta-glycoside hydrolase, the Cel5A from Bacillus agaradhaerens, is, presented in which the structures of each of the native, substrate, covalent-intermediate, and product complexes have been determined and, their interconversions analyzed kinetically, providing unprecedented, insights into the mechanism of this enzyme class. Substrate is bound in a, distorted 1S3 skew-boat conformation, thereby presenting the anomeric, carbon appropriately for nucleophilic attack as well as satisfying the, stereoelectronic requirements for an incipient oxocarbenium ion. Leaving, group departure results in ... [(full description)]

About this Structure

4A3H is a [Single protein] structure of sequence from [Bacillus agaradhaerens] with DCB as [ligand]. Active as [[1]], with EC number [3.2.1.4]. Full crystallographic information is available from [OCA].

Reference

Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase., Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG, Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:9718293

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