ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Unexpected features in the Protein Data Bank entries 3qd1 and 4i8e: the structural description of the binding of the serine-rich repeat adhesin GspB to host cell carbohydrate receptor is not a solved issue.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 8 citations in OpenAlex.
- A high-resolution data set of fatty acid-binding protein structures. III. Unexpectedly high occurrence of wrong ligands.Acta crystallographica. Section D, Structural biology · 2025Article
- Structural basis for the role of serine-rich repeat proteins fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Detect, correct, retract: How to manage incorrect structural models.The FEBS journal · 2018Review
- Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.The Journal of biological chemistry · 2017Article
- Models of protein-ligand crystal structures: trust, but verify.Journal of computer-aided molecular design · 2015Article
- The solvent component of macromolecular crystals.Acta crystallographica. Section D, Biological crystallography · 2015Review
- Automated identification of crystallographic ligands using sparse-density representations.Acta crystallographica. Section D, Biological crystallography · 2014Article
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1 author at 1 institution in 1 country.
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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.
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