1aiw | pdb_00001aiw

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

spinqualitylabelsall models 1aiw, 23 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aiw is a 1 chain structure with sequence from Dicd3. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CELZ (DICD3) Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [GUNZ_DICD3] Represents 97% of the global cellulase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 a conformation compatible with a cellulose-binding site. Based on its original folding, we have been able to relate the CBD sequence to those of several domains of unknown function occurring in several bacterial chitinases as well as other proteins. This study also provides a structural basis for analyzing the secretion-related information specific to the CBDEGZ. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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