Summary for 7SMH
| Entry DOI | 10.2210/pdb7smh/pdb |
| Related | 7sie |
| Descriptor | Surface protein G, CALCIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | cell adhesion, l-type lectin |
| Biological source | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Total number of polymer chains | 4 |
| Total formula weight | 123109.29 |
| Authors | Atkin, K.E.,Whelan, F.,Brentnall, A.S.,Dodson, E.J.,Turkenburg, J.P.,Potts, J.R. (deposition date: 2021-10-25, release date: 2022-11-02, Last modification date: 2023-10-25) |
| Primary citation | Clark, L.C.,Atkin, K.E.,Whelan, F.,Brentnall, A.S.,Harris, G.,Towell, A.M.,Turkenburg, J.P.,Liu, Y.,Feizi, T.,Griffiths, S.C.,Geoghegan, J.A.,Potts, J.R. Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface. J.Biol.Chem., 299:102936-102936, 2023 Cited by PubMed Abstract: Staphylococcus aureus and Staphylococcus epidermidis are frequently associated with medical device infections that involve establishment of a bacterial biofilm on the device surface. Staphylococcal surface proteins Aap, SasG, and Pls are members of the Periscope Protein class and have been implicated in biofilm formation and host colonization; they comprise a repetitive region ("B region") and an N-terminal host colonization domain within the "A region," predicted to be a lectin domain. Repetitive E-G5 domains (as found in Aap, SasG, and Pls) form elongated "stalks" that would vary in length with repeat number, resulting in projection of the N-terminal A domain variable distances from the bacterial cell surface. Here, we present the structures of the lectin domains within A regions of SasG, Aap, and Pls and a structure of the Aap lectin domain attached to contiguous E-G5 repeats, suggesting the lectin domains will sit at the tip of the variable length rod. We demonstrate that these isolated domains (Aap, SasG) are sufficient to bind to human host desquamated nasal epithelial cells. Previously, proteolytic cleavage or a deletion within the A domain had been reported to induce biofilm formation; the structures suggest a potential link between these observations. Intriguingly, while the Aap, SasG, and Pls lectin domains bind a metal ion, they lack the nonproline cis peptide bond thought to be key for carbohydrate binding by the lectin fold. This suggestion of noncanonical ligand binding should be a key consideration when investigating the host cell interactions of these bacterial surface proteins. PubMed: 36702253DOI: 10.1016/j.jbc.2023.102936 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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