@article {444,
	title = {Carbohydrate-binding modules recognize fine substructures of cellulose},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {52},
	year = {2002},
	note = {ISI Document Delivery No.: 631QDTimes Cited: 20Cited Reference Count: 36},
	month = {Dec},
	pages = {50245-50254},
	type = {Article},
	abstract = {Competition isotherms are used to identify the set of cellulose substructures to which cellulose binding modules (CBMs) from families 2a, 3, 4, 9, and 17 bind. The experiments are based on coupling a unique fluorescent tag to each CBM in a manner that does not alter the natural binding properties of the CBM and therefore allows the surface and solution concentrations of each CBM to be monitored as a function of time and composition. Adsorption and surface exchange of like or competing CBMs are monitored using a range of cellulose preparations varying in both crystallinity and provenance. CBMs from families 2a, 3,4,9, and 17 are shown to recognize different physical forms of prepared cellulose. The demonstration of the very fine binding specificity of cellulose-specific CBMs implies that the polysaccharide targets of CBMs extend down to the resolution of cellulose microstructures.},
	keywords = {BACTERIAL, CELLULASE, CRYSTALLINE CELLULOSE, DOMAIN, EXOGLUCANASE, FIMI CENC, NMR-SPECTROSCOPY, PROTEIN-A, SPECIFICITY, TRYPTOPHAN RESIDUES, XYLANASE 10A},
	isbn = {0021-9258},
	url = {<Go to ISI>://000180177700007},
	author = {McLean, B. W. and Boraston, A. B. and Brouwer, D. and Sanaie, N. and Fyfe, C. A. and Warren, R. A. J. and Kilburn, D. G. and Haynes, C. A.}
}
@article {4856,
	title = {Binding site analysis of cellulose binding domain CBDN1 from endoglucanse C of Cellulomonas fimi by site-directed mutagenesis},
	journal = {Biochemistry},
	volume = {39},
	number = {30},
	year = {2000},
	note = {ISI Document Delivery No.: 339RJTimes Cited: 17Cited Reference Count: 59},
	month = {Aug},
	pages = {8844-8852},
	type = {Article},
	abstract = {Endoglucanase C (CenC), a beta 1,4 glucanase from the soil bacterium Cellulomonas fimi, binds to amorphous cellulose via two homologous cellulose binding domains, termed CBDN1 and CBDN2. in this work, the contributions of 10 amino acids within the binding cleft of CBDN1 were evaluated by single site-directed mutations to alanine residues. Each isolated domain containing a single mutation was analyzed for binding to an insoluble amorphous preparation of cellulose, phosphoric acid swollen Avicel (PASA), and to a soluble glucopyranoside polymer, barley beta-glucan. The effect of any given mutation on CBD binding was similar for both substrates, suggesting that the mechanism of binding to soluble and insoluble substrates is the same. Tyrosines 19 and 85 were essential for tight binding by CBDN1 as their replacement by alanine results in affinity decrements of approximately 100-fold on PASA, barley beta-glucan, and soluble cellooligosaccharides. The tertiary structures of unbound Y19A and Y85A were assessed by heteronuclear single quantum coherence (HSQC) spectroscopy. These studies indicated that the structures of both mutants were perturbed but that all perturbations are very near to the site of mutation.},
	keywords = {4-GLUCANASE CENC, BETA-1, ESCHERICHIA-COLI, LIGAND-BINDING, LIMITED PROTEOLYSIS, MECHANISM, N-ACETYLGLUCOSAMINE, NUCLEAR-MAGNETIC-RESONANCE, REESEI CELLOBIOHYDROLASE-I, TRICHODERMA-REESEI, TRYPTOPHAN RESIDUES},
	isbn = {0006-2960},
	url = {<Go to ISI>://000088491500018},
	author = {Kormos, J. and Johnson, P. E. and Brun, E. and Tomme, P. and McIntosh, L. P. and Haynes, C. A. and Kilburn, D. G.}
}
@article {3708,
	title = {Interaction of soluble cellooligosaccharides with the N-terminal cellulose-binding domain of Cellulomonas fimi CenC .2. NMR and ultraviolet absorption spectroscopy},
	journal = {Biochemistry},
	volume = {35},
	number = {44},
	year = {1996},
	note = {ISI Document Delivery No.: VR098Times Cited: 68Cited Reference Count: 46},
	month = {Nov},
	pages = {13895-13906},
	type = {Article},
	abstract = {The N-terminal cellulose-binding domain (CBDN1) from Cellulomonas fimi beta-1,4-glucanase CenC binds amorphous but not crystalline cellulose. To investigate the structural and thermodynamic bases of cellulose binding, NMR and difference ultraviolet absorbance spectroscopy were used in parallel with calorimetry (Tomme, P., Creagh, A. L., Kilburn, D. G., \& Haynes, C. A., (1996) Biochemistry 35, 13885-13894] to characterize the interaction of soluble cellooligosaccharides with CBDN1 Association constants, determined from the dependence of the amide H-1 and N-15 chemical shifts of CBDN1 upon added sugar, increase from 180 +/- 60 M(-1) for cellotriose to 4 200 +/- 720 M(-1) for cellotetraose, 34 000 +/- 7 600 M(-1) for cellopentaose, and an estimate of 50 000 M(-1) for cellohexaose. This implies that the CBDN1 cellulose-binding site spans approximately five glucosyl units, On the basis of the observed patterns of amide chemical shift changes, the cellooligosaccharides bind along a five-stranded beta-sheet that forms a concave face of the jelly-roll beta-sandwich structure of CBDN1. This beta-sheet contains a strip of hydrophobic side chains flanked on both sides by polar residues, NMR and difference ultraviolet absorbance measurements also demonstrate that tyrosine, but not tryptophan, side chains may be involved in oligosaccharide binding. These results lead to a model in which CBDN1 interacts with soluble cellooligosaccharides and, by inference, with single polysaccharide chains in regions of amorphous cellulose, primarily through hydrogen bonding to the equatorial hydroxyl groups of the pyranose rings. Van der against the apolar side chains may augment binding. CBDN1 stands in marked contrast to previously characterized CBDs that absorb to crystalline cellulose via a flat binding surface dominated by exposed aromatic rings.},
	keywords = {BACKBONE H-1, CHEMICAL-SHIFTS, ESCHERICHIA-COLI, EXPRESSION, HIGH-LEVEL, NUCLEAR-MAGNETIC-RESONANCE, PROTEIN, REESEI CELLOBIOHYDROLASE-I, SEQUENCE, TRICHODERMA-REESEI, TRYPTOPHAN RESIDUES},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1996VR09800005},
	author = {Johnson, P. E. and Tomme, P. and Joshi, M. D. and McIntosh, L. P.}
}
