3pnt: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/D7S065_STRPY D7S065_STRPY] | [https://www.uniprot.org/uniprot/D7S065_STRPY D7S065_STRPY] | ||
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== 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<ref>PMID:21300288</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||