@article {4745,
	title = {Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C},
	journal = {Biochemistry},
	volume = {39},
	number = {10},
	year = {2000},
	note = {ISI Document Delivery No.: 294HFTimes Cited: 31Cited Reference Count: 74},
	month = {Mar},
	pages = {2445-2458},
	type = {Article},
	abstract = {The 1,4-beta-glucanase CenC from Cellulomonas fimi contains two cellulose-binding domains, CBDN1 and CBDN2, arranged in tandem at its N-terminus. These homologous CBDs are distinct in their selectivity for binding amorphous and not crystalline cellulose. Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of CBDN2 in the presence of saturating amounts of cellopentaose. A total of 1996 experimental restraints were used to calculate an ensemble of 21 final structures for the protein. CBDN2 is composed of 11 beta-strands, folded into two antiparallel beta-sheets, with a topology of a jellyroll beta-sandwich. On the basis of patterns of chemical shift perturbations accompanying the addition of cellooligosaccharides, as well as the observation of intermolecular protein-sugar NOE interactions, the cellulose-binding site of CBDN2 was identified as a cleft that lies across one face of the beta-sandwich. The thermodynamic basis for the binding of cellooligosaccharides was investigated using isothermal titration calorimetry and NMR spectroscopy. Binding is enthalpically driven and consistent with a structural model involving hydrogen bonding between the equatorial hydroxyls of the glucopyranosyl rings and polar amino acid side chains lining the CBDN2 cleft. Affinity electrophoresis was used to determine that CBDN2 also binds soluble beta-1,4-linked polymers of glucose, including hydroxyethylcellulose and beta-1,3-1,4-glucans. This study complements a previous analysis of CBDN1 [Johnson, P. E., Joshi, M. D., Tomme, P., Kilburn, D. G., and McIntosh, L. P. (1996) Biochemistry 35, 14381-14394] and demonstrates that the homologous CBDs from CenC share very similar structures and sugar binding properties.},
	keywords = {3-DIMENSIONAL SOLUTION STRUCTURE, C-13-ENRICHED PROTEINS, C-13-LABELED PROTEINS, CHEMICAL-SHIFT, DISTANCE GEOMETRY, IMPROVED SENSITIVITY, INDEX, ISOTOPICALLY-ENRICHED PROTEINS, LARGER PROTEINS, NUCLEAR-MAGNETIC-RESONANCE, SIDE-CHAIN RESONANCES},
	isbn = {0006-2960},
	url = {<Go to ISI>://000085905300003},
	author = {Brun, E. and Johnson, P. E. and Creagh, A. L. and Tomme, P. and Webster, P. and Haynes, C. A. and McIntosh, L. P.}
}
@article {3707,
	title = {Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy},
	journal = {Biochemistry},
	volume = {35},
	number = {45},
	year = {1996},
	note = {ISI Document Delivery No.: VT081Times Cited: 94Cited Reference Count: 90},
	month = {Nov},
	pages = {14381-14394},
	type = {Article},
	abstract = {Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of the 152 amino acid N-terminal cellulose-binding domain from Cellulomonas fimi 1,4-beta-glucanase CenC (CBDN1) CBDN1 was studied in the presence of saturating concentrations of cellotetraose, but due to spectral overlap, the oligosaccharide was not included in the structure calculations. A total of 1705 interproton nuclear Overhauser effect (NOE), 56 phi, 88 psi, 42 chi 1, 9 chi 2 dihedral angle, and 88 hydrogen-bond restraints were used to calculate 25 final structures. These structures have a rmsd from the average of 0.79 +/- 0.11 Angstrom for all backbone atoms excluding disordered termini and 0.44 +/- 0.05 Angstrom for residues with regular secondary structures. CBDN1 is composed of 10 beta-strands, folded into two antiparallel beta-sheets with the topology of a jelly-roll beta-sandwich. The strands forming the face of the protein previously determined by chemical shift perturbations to be responsible for cellooligosaccharide binding [Johnson, P. E., Tomme, P., Joshi, M. D., \& McIntosh, L. P. (1996) Biochemistry, 35, 13895-13906] are shorter than those forming the opposite side of the protein. This results in a 5-stranded binding cleft, containing a central strip of hydrophobic residues that is flanked on both sides by polar hydrogen-bonding groups. The presence of this cleft provides a structural explanation for the unique selectivity of CBDN1 for amorphous cellulose and other soluble oligosaccharides and the lack of binding to crystalline cellulose, The tertiary structure of CBDN1 is strikingly similar to that of the bacterial 1,3-1,4-beta-glucanases, as well as other sugar-binding proteins with jelly-roll folds.},
	keywords = {3-DIMENSIONAL SOLUTION STRUCTURE, C-13-ENRICHED PROTEINS, CHEMICAL-SHIFT, DISTANCE GEOMETRY, INDEX, ISOTOPICALLY-ENRICHED PROTEINS, LARGER PROTEINS, NMR-SPECTROSCOPY, REESEI CELLOBIOHYDROLASE-I, SIDE-CHAIN RESONANCES, TRICHODERMA-REESEI},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1996VT08100039},
	author = {Johnson, P. E. and Joshi, M. D. and Tomme, P. and Kilburn, D. G. and McIntosh, L. P.}
}
