Abstract
The structure of a complex between a fragment of the adhesin GspB from Streptococcus gordonii and a disaccharide (PDB entries 3qd1 and 4i8e) has recently been proposed to identify the binding site for the sialyl-T antigen recognized by GspB. This structure exhibits numerous unrealistic and unusual features such as an excessive number of van der Waals clashes and a lack of correlation between atomic structure and experimental electron density. Here, it is shown that the crystallographic data can be fully explained by an alternative model, namely replacing the disaccharide with a buffer molecule. The conclusion is that the experimental data are likely to contain no information regarding the carbohydrate receptor binding site in GspB or the interaction of GspB with host cell receptors.