1aiw

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[[Category: erwinia chrysanthemi]]
[[Category: erwinia chrysanthemi]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:32:41 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:48:47 2007''

Revision as of 12:44, 30 October 2007


1aiw

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NMR STRUCTURES OF THE CELLULOSE-BINDING DOMAIN OF THE ENDOGLUCANASE Z FROM ERWINIA CHRYSANTHEMI, 23 STRUCTURES

Overview

Two-dimensional proton nuclear magnetic resonance spectroscopy has been, used to determine the three-dimensional structure of the 62 amino acid, C-terminal cellulose-binding domain (CBD) of the endoglucanase Z (CBDEGZ), secreted by Erwinia chrysanthemi. An experimental data set comprising 958, interproton nOe-derived restraints was used to calculate 23 structures., The calculated structures have an average root-mean-square deviation, between Cys4 and Cys61 of 0.91 +/- 0.11 A for backbone atoms and 1.18 +/-, 0.12 A for the heavy atoms. The CBDEGZ exhibits a skiboot shape based, mainly on a triple antiparallel beta-sheet perpendicular to a less-ordered, summital loop. Three aromatic rings (Trp18, Trp43, and Tyr44) are, localized on one face of the protein and are exposed to the solvent in ... [(full description)]

About this Structure

1AIW is a [Single protein] structure of sequence from [Erwinia chrysanthemi]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

Reference

Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi., Brun E, Moriaud F, Gans P, Blackledge MJ, Barras F, Marion D, Biochemistry. 1997 Dec 23;36(51):16074-86. PMID:9405041

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