The glucodextranase B domain adopts a structure consisting of seven/eight-strand antiparallel beta-sheets, in a Greek-key topology, similar to the immunoglobulin beta-sandwich fold. It acts as a cell wall anchor, interacting with the S-layer present in the cell wall of Gram-positive bacteria by hydrophobic interactions. In glucodextranase, domain B is buried in the S-layer, and a flexible linker located between domain B and the catalytic unit confers motion to the catalytic unit, which is capable of efficient hydrolysis of the substrates located close to the cell surface [1].
Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y.
Structural insights into substrate specificity and function of glucodextranase.
J. Biol. Chem. 279 10575-83 2004
[PubMed: 14660574] http://dx.doi.org/10.1074/jbc.M310771200