3PNT
Crystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPN
Summary for 3PNT
| Entry DOI | 10.2210/pdb3pnt/pdb |
| Related | 3QB2 |
| Descriptor | NAD+-glycohydrolase, Immunity factor for SPN (3 entities in total) |
| Functional Keywords | glycohydrolase, nad+, virulence factor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Streptococcus pyogenes More |
| Total number of polymer chains | 4 |
| Total formula weight | 100755.42 |
| Authors | Smith, C.L.,Stine Elam, J.,Ellenberger, T.,Ghosh, J.,Pinkner, J.S.,Hultgren, S.J.,Caparon, M.G. (deposition date: 2010-11-19, release date: 2011-03-02, Last modification date: 2024-11-27) |
| Primary citation | Smith, C.L.,Ghosh, J.,Elam, J.S.,Pinkner, J.S.,Hultgren, S.J.,Caparon, M.G.,Ellenberger, T. Structural Basis of Streptococcus pyogenes Immunity to Its NAD(+) Glycohydrolase Toxin. Structure, 19:192-202, 2011 Cited by PubMed Abstract: The virulence of Gram-positive bacteria is enhanced by toxins like the Streptococcus pyogenes β-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 β-NAD(+). The protective effect of IFS involves an extensive interaction with the SPN active site that blocks access to β-NAD(+). The conformation of IFS changes upon binding to SPN, with repacking of an extended C-terminal α 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. PubMed: 21300288DOI: 10.1016/j.str.2010.12.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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