8tb2

Structure of SasG (type II) (residues 165-421) from Staphylococcus aureus MW2

spinqualitylabelsall models 8tb2, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8tb2 is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus MW2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: CA, NA, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLS_STAAW Publication Abstract from PubMed Staphylococcus aureus causes the majority of skin and soft tissue infections, but this pathogen only transiently colonizes healthy skin. However, this transient skin exposure enables S. aureus to transition to infection. The initial adhesion of S. aureus to skin corneocytes is mediated by surface protein G (SasG). Here, phylogenetic analyses reveal the presence of two major divergent SasG alleles in S. aureus: SasG-I and SasG-II. Structural analyses of SasG-II identify a nonaromatic arginine in the binding pocket of the lectin subdomain that mediates adhesion to corneocytes. Atomic force microscopy and corneocyte adhesion assays indicate that SasG-II can bind to a broader variety of ligands than SasG-I. Glycosidase treatment results in different binding profiles between SasG-I and SasG-II on skin cells. In addition, SasG-mediated adhesion is recapitulated using differentiated N/TERT keratinocytes. Our findings indicate that SasG-II has evolved to adhere to multiple ligands, conferring a distinct advantage to S. aureus during skin colonization. Staphylococcus aureus skin colonization is mediated by SasG lectin variation.,Mills KB, Maciag JJ, Wang C, Crawford JA, Enroth TJ, Keim KC, Dufrene YF, Robinson DA, Fey PD, Herr AB, Horswill AR Cell Rep. 2024 Apr 23;43(4):114022. doi: 10.1016/j.celrep.2024.114022. Epub 2024 , Apr 2. PMID:38568806 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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