Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy

The structure of the N-terminal cellulose-binding domain from Cellulomonas fimi 1,4-beta-glucanase CenC was determined by multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results revealed 10 beta-strands which were folded into two antiparallel beta-sheets, forming a jelly-roll beta-sandwich. The strands of the protein surface were shorter than those found in the opposite side of the protein, resulting in a five-stranded binding cleft containing hydrophobic residues at the center and flanked by polar hydrogen-bonding groups.