IUCr journals

Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus

Acta Cryst. (2012). F68, 8–13 (http://doi.org/fx9pds)

[CBM3b]  Planar face of the CBM3b module from the cellulosome of Acetivibrio cellulolyticus. Cellulose-binding residues are indicated.

Selected anaerobic bacteria produce a multienzyme cellulosome complex that degrades cellulose. Carbohydrate-binding modules (CBM) target these cellulolytic protein complexes to the cellulose substrate. The binding interaction is driven by a characteristic pattern of aromatic side chains and salt bridges located on a planar surface of the CBM. The structure of the CBM3b from Acetivibrio cellulolyticus reveals a particularly compact interacting region consisting of only four amino-acid residues.

O. Yaniv, Y. Halfon, L. J. W. Shimon, E. A. Bayer, R. Lamed and F. Frolow