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Structure of Ltp, a superinfection exclusion protein from the Streptococcus thermophilus temperate phage TP-J34Structure of Ltp, a superinfection exclusion protein from the Streptococcus thermophilus temperate phage TP-J34
Structural highlights
Publication Abstract from PubMedLipoproteins of temperate phage are a broad family of membrane proteins encoded in the lysogeny module of temperate phages. Expression of the ltpTP - J 34 gene of temperate Streptococcus thermophilus phage TP-J34 interferes with phage infection at the stage of triggering DNA release and injection into the cell. Here, we report the first structure of a superinfection exclusion protein. We have expressed and determined the X-ray structure of LtpTP - J 34 . The soluble domain of LtpTP - J 34 is composed of a tandem of three-helix helix-turn-helix (HTH) domains exhibiting a highly negatively charged surface. By isolating mutants of lactococcal phage P008wt with reduced sensitivities to LtpTP -J34 and by genome sequencing of such mutants we obtained evidence supporting the notion that LtpTP - J 34 targets the phage's tape measure protein (TMP) and blocks its insertion into the cytoplasmic membrane. X-ray structure of a superinfection exclusion lipoprotein from phage TP-J34 and identification of the tape measure protein as its target.,Bebeacua C, Lorenzo Fajardo JC, Blangy S, Spinelli S, Bollmann S, Neve H, Cambillau C, Heller KJ Mol Microbiol. 2013 Jul;89(1):152-65. doi: 10.1111/mmi.12267. Epub 2013 Jun 7. PMID:23692331[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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