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1ovw
From Proteopedia
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(New page: 200px<br /> <applet load="1ovw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ovw, resolution 2.7Å" /> '''ENDOGLUCANASE I COMP...)
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Revision as of 19:28, 29 October 2007
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ENDOGLUCANASE I COMPLEXED WITH NON-HYDROLYSABLE SUBSTRATE ANALOGUE
Overview
Endoglucanase I (EG I) is a cellulase, from glycosyl hydrolase family 7, which cleaves the beta-1,4 linkages of cellulose with overall retention of, configuration. The structure of the EG I from Fusarium oxysproum, complexed to a nonhydrolyzable thiooligosaccharide substrate analogue, has, been determined by X-ray crystallography at a resolution of 2.7 A, utilizing the 4-fold noncrystallographic symmetry present in the, asymmetric unit. The electron density map clearly reveals the presence of, three glucosyl units of the inhibitor, consistent with the known number of, sugar-binding subsites, located at the active site of the enzyme in the, -2, -1, and +1 subsites, i.e., actually spanning the point of enzymatic, cleavage. The pyranose ring at the point of potential enzymatic cleavage, is ... [(full description)]
About this Structure
1OVW is a [Single protein] structure of sequence from [Fusarium oxysporum] with NAG and DP5 as [ligands]. Active as [[1]], with EC number [3.2.1.4]. Full crystallographic information is available from [OCA].
Reference
Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group., Sulzenbacher G, Driguez H, Henrissat B, Schulein M, Davies GJ, Biochemistry. 1996 Dec 3;35(48):15280-7. PMID:8952478
Page seeded by OCA on Mon Oct 29 21:32:40 2007
