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-Structure paper
タイトル | Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in gram-positive infecting phages. |
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ジャーナル・号・ページ | J Biol Chem, Vol. 285, Issue 47, Page 36666-36673, Year 2010 |
掲載日 | 2010年11月19日 |
![]() | David Veesler / Gautier Robin / Julie Lichière / Isabelle Auzat / Paulo Tavares / Patrick Bron / Valérie Campanacci / Christian Cambillau / ![]() |
PubMed 要旨 | Siphophage SPP1 infects the gram-positive bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low resolution assignment of most ...Siphophage SPP1 infects the gram-positive bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low resolution assignment of most orf products belonging to these regions. We report here the structure of the SPP1 distal tail protein (Dit, gp19.1). The combination of x-ray crystallography, EM, and light scattering established that Dit is a back-to-back dimer of hexamers. However, Dit fitting in the virion EM maps was only possible with a hexamer located between the tail-tube and the tail-tip. Structure comparison revealed high similarity between Dit and a central component of lactophage baseplates. Sequence similarity search expanded its relatedness to several phage proteins, suggesting that Dit is a docking platform for the tail adsorption apparatus in Siphoviridae infecting gram-positive bacteria and that its architecture is a paradigm for these hub proteins. Dit structural similarity extends also to non-contractile and contractile phage tail proteins (gpV(N) and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.95 - 21.5 Å |
構造データ | ![]() EMDB-1779: ![]() PDB-2x8k: |
由来 |
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![]() | VIRAL PROTEIN / DISTAL TAIL PROTEIN |