8deo

Structure of AAP A domain and B-repeats (residues 351-813) from Staphylococcus epidermidis

spinqualitylabelsall models 8deo, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8deo is a 2 chain structure with sequence from Staphylococcus epidermidis RP62A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CA, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5HKE8_STAEQ Publication Abstract from PubMed 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. Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface.,Clark LC, Atkin KE, Whelan F, Brentnall AS, Harris G, Towell AM, Turkenburg JP, Liu Y, Feizi T, Griffiths SC, Geoghegan JA, Potts JR J Biol Chem. 2023 Mar;299(3):102936. doi: 10.1016/j.jbc.2023.102936. Epub 2023 , Jan 24. PMID:36702253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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