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1aiw
From Proteopedia
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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 [[1]], with EC number [3.2.1.4]. 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
Page seeded by OCA on Mon Oct 29 18:03:19 2007
