4EQQ

Structure of Ltp, a superinfection exclusion protein from the Streptococcus thermophilus temperate phage TP-J34

Summary for 4EQQ

• Entry DOI: 10.2210/pdb4eqq/pdb
• Descriptor: Putative host cell surface-exposed lipoprotein, SULFATE ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: hth fold, superinfection exclusion, lipoprotein ektodomain, protein binding
• Biological source: Streptococcus phage TP-J34
• Total number of polymer chains: 2
• Total formula weight: 25282.79

Authors

Bebeacua, C.,Lorenzo, C.,Blangy, S.,Spinelli, S.,Heller, K.,Cambillau, C. (deposition date: 2012-04-19, release date: 2013-06-05, Last modification date: 2024-02-28)

Primary citation

Bebeacua, C.,Lorenzo Fajardo, J.C.,Blangy, S.,Spinelli, S.,Bollmann, S.,Neve, H.,Cambillau, C.,Heller, K.J.
X-ray structure of a superinfection exclusion lipoprotein from phage TP-J34 and identification of the tape measure protein as its target.
Mol.Microbiol., 89:152-165, 2013

PubMed Abstract: Lipoproteins of temperate phage are a broad family of membrane proteins encoded in the lysogeny module of temperate phages. Expression of the ltp(TP-J34) 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 Ltp(TP-J34). The soluble domain of Ltp(TP-J34) 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 Ltp(TP-J34) and by genome sequencing of such mutants we obtained evidence supporting the notion that Ltp(TP-J34) targets the phage's tape measure protein (TMP) and blocks its insertion into the cytoplasmic membrane.

PubMed: 23692331
DOI: 10.1111/mmi.12267

Experimental method

X-RAY DIFFRACTION (2.05 Å)