6dq3

Streptococcus pyogenes deacetylase PplD in complex with acetate

spinqualitylabelsall models 6dq3, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dq3 is a 2 chain structure with sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: ACT, EDO, IMD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function J7M3C9_STRP1 Publication Abstract from PubMed The cell wall of the human bacterial pathogen Group A Streptococcus (GAS) consists of peptidoglycan decorated with the Lancefield group A carbohydrate (GAC). GAC is a promising target for the development of GAS vaccines. In this study, employing chemical, compositional, and NMR methods, we show that GAC is attached to peptidoglycan via glucosamine 1-phosphate. This structural feature makes the GAC-peptidoglycan linkage highly sensitive to cleavage by nitrous acid and resistant to mild acid conditions. Using this characteristic of the GAS cell wall, we identify PplD as a protein required for deacetylation of linkage N-acetylglucosamine (GlcNAc). X-ray structural analysis indicates that PplD performs catalysis via a modified acid/base mechanism. Genetic surveys in silico together with functional analysis indicate that PplD homologs deacetylate the polysaccharide linkage in many streptococcal species. We further demonstrate that introduction of positive charges to the cell wall by GlcNAc deacetylation protects GAS against host cationic antimicrobial proteins. PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides.,Rush JS, Parajuli P, Ruda A, Li J, Pohane AA, Zamakhaeva S, Rahman MM, Chang JC, Gogos A, Kenner CW, Lambeau G, Federle MJ, Korotkov KV, Widmalm G, Korotkova N Nat Commun. 2022 Feb 1;13(1):590. doi: 10.1038/s41467-022-28257-0. PMID:35105886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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