How FMN binds to anabaena apoflavodoxin: a hydrophobic encounter at an open binding site.

Molecular recognition begins when two molecules approach and establish interactions of certain strength. The mechanisms of molecular recognition reactions between biological molecules are not well known, and few systems have been analyzed in detail. We investigate here the reaction between an apoprotein and its physiological cofactor (apoflavodoxin and flavin mononucleotide) that binds reversibly to form a non-covalent complex (flavodoxin) involved in electron transfer reactions.

Expression, crystallization and preliminary X-ray diffraction studies on the complete choline-binding domain of the major pneumococcal autolysin.

The major pneumococcal autolysin (LytA), a virulence factor of this bacterium, is composed of an amino-terminal catalytic domain plus a carboxyl-terminal choline-binding domain (ChBD). This C-terminal domain, responsible for anchorage to the cell wall, is a tandem of six imperfect 20-residue repeats whose precise ends have been difficult to establish by sequence methods. The reported crystal structure of a shortened C-terminal fragment of the protein suggested that it might contain an additional repeat and thus an additional choline-binding site (ChBS).