6leb

Staphylococcus aureus surface protein SdrC mutant-P366H

spinqualitylabelsall models 6leb, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6leb is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Ligands: GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2UWK0_STAAU Publication Abstract from PubMed Staphylococcus aureus is an opportunistic disease-causing pathogen that is widely found in the community and on medical equipment. A series of virulence factors secreted by S. aureus can trigger severe diseases such as sepsis, endocarditis and toxic shock, and thus have a great impact on human health. The transformation of S. aureus from a colonization state to a pathogenic state during its life cycle is intimately associated with the initiation of bacterial aggregation and biofilm accumulation. SdrC, an S. aureus surface protein, can act as an adhesin to promote cell attachment and aggregation by an unknown mechanism. Here, structural studies demonstrate that SdrC forms a unique dimer through intermolecular interaction. It is proposed that the dimerization of SdrC enhances the efficiency of bacteria-host attachment and therefore contributes to the pathogenicity of S. aureus. Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus.,Wang J, Zhang M, Wang M, Zang J, Zhang X, Hang T Acta Crystallogr F Struct Biol Commun. 2021 Feb 1;77(Pt 2):47-53. doi:, 10.1107/S2053230X21000741. Epub 2021 Feb 2. PMID:33620037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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