3pnt

Crystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPN

spinqualitylabelsall models 3pnt, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pnt is a 4 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 2.8Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D7S065_STRPY Publication Abstract from PubMed The virulence of Gram-positive bacteria is enhanced by toxins like the Streptococcus pyogenes beta-NAD(+) glycohydrolase known as SPN. SPN-producing strains of S. pyogenes additionally express the protein immunity factor for SPN (IFS), which forms an inhibitory complex with SPN. We have determined crystal structures of the SPN-IFS complex and IFS alone, revealing that SPN is structurally related to ADP-ribosyl transferases but lacks the canonical binding site for protein substrates. SPN is instead a highly efficient glycohydrolase with the potential to deplete cellular levels of beta-NAD(+). The protective effect of IFS involves an extensive interaction with the SPN active site that blocks access to beta-NAD(+). The conformation of IFS changes upon binding to SPN, with repacking of an extended C-terminal alpha helix into a compact shape. IFS is an attractive target for the development of novel bacteriocidal compounds functioning by blocking the bacterium's self-immunity to the SPN toxin. Structural Basis of Streptococcus pyogenes Immunity to Its NAD(+) Glycohydrolase Toxin.,Smith CL, Ghosh J, Elam JS, Pinkner JS, Hultgren SJ, Caparon MG, Ellenberger T Structure. 2011 Feb 9;19(2):192-202. PMID:21300288 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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