The X-Ray Crystal Structure of the Phage λ Tail Terminator Protein Reveals the Biologically Relevant Hexameric Ring Structure and Demonstrates a Conserved Mechanism of Tail Termination among Diverse Long-Tailed Phages

Pell, Lisa G; Liu, Amanda; Edmonds, Lizbeth; Donaldson, Logan W.; Howell, P. Lynne; Davidson, Alan R.

doi:10.1016/j.jmb.2009.04.072

Cited by 57 publications

(75 citation statements)

References 53 publications

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“…All three protein domains share a similar fold made of two antiparallel ␤-sheets arranged in two layers plus an ␣-helix. This finding reinforces and extends the previously proposed hypothesis that contractile and non-contractile phage tails may have an evolutionary connection (6,7). Considering the high structural conservation observed among proteins involved in the assembly of different parts of the tail as well as their belonging to distant phage families (Siphoviridae and Myoviridae), we suggest that most phage tail components derived from an unique ancestral protein module, which has evolved to provide all these different proteins.…”

Section: Dit a Hub In Siphoviridae Infecting Gram-positive Bacteria-supporting

confidence: 92%

“…EVPC is most probably homologous to Hcp1/Hcp3 as suggested by their high amino acid sequence identities (32/21%), similarities (49/40%), and their structural resemblance (supplemental Table S2). These results constitute additional evidence for an evolutionary relationship between components of the T6SS and phage tails as was previously proposed based on the observed structural similarity between the phage gpV N and P. aeruginosa Hcp1 (6,39) and between the phage T4 gp27 and E. coli VgrG (40).…”

Section: Dit a Hub In Siphoviridae Infecting Gram-positive Bacteria-supporting

confidence: 86%

“…This feature facilitates DNA traffic into the host cytoplasm during infection and prevents interactions with the channel wall. A similar negatively charged conduit is observed in the SPP1 head-to-tail connector channel (37) as well as in the phage tail-terminator channel (6). The interface buried surface area between two neighboring monomers within a Dit hexameric ring is ϳ1,300 Å 2 per monomer (ϳ10% of the monomer surface).…”

Section: Dit Production and Light Scattering Characterization-spp1supporting

confidence: 52%

“…In phages of Gram-positive bacteria this structure is composed of the distal tail protein (Dit), the tail fiber, and eventually ancillary proteins, all forming the baseplate (4). Although three-dimensional structures of siphophages MTP (5) and tail terminator (6) have been reported, no high-resolution structure is available for components of the adsorption device with the exception of our recently reported phage p2 baseplate structure (7). Several tail components of the Bacillus subtilis phage SPP1 show significant sequence similarity to equivalent proteins from lactococcal phages Tuc2009 and TP901-1.…”

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confidence: 99%

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Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

Veesler

Robin

Lichière

et al. 2010

Journal of Biological Chemistry

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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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Section: Dit a Hub In Siphoviridae Infecting Gram-positive Bacteria-supporting

confidence: 92%

Section: Dit a Hub In Siphoviridae Infecting Gram-positive Bacteria-supporting

confidence: 86%

Section: Dit Production and Light Scattering Characterization-spp1supporting

confidence: 52%

mentioning

confidence: 99%

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Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

Veesler

Robin

Lichière

et al. 2010

Journal of Biological Chemistry

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“…5), which form closed ring structures found as a part of the tail tube, neck, or baseplate (19). This β-sandwich fold is observed, for example, in a bacteriophage T4 baseplate protein gp27, lambda tail tube protein gpV, lambda neck protein gpU, and gpFII (48)(49)(50)(51). Most of these proteins are hexamers or pseudo-hexamers (i.e., trimers with a monomer that has domain duplication) like gp27 of T4.…”

Section: Resultsmentioning

confidence: 97%

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

Aksyuk

Bowman

Kaufmann

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T ¼ 4 icosahedral lattice. The C1 tail is terminated with a φ29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.bacteriophage C1 tail | tail knob | X-ray crystallography

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NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage‐related protein family PF13554

et al. 2011

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The solution structure of the hypothetical phage-related protein NP_888769.1 from the Gram-negative bacterium Bordetella bronchoseptica contains a well-structured core comprising a five-stranded, antiparallel b-sheet packed on one side against two a-helices and a short b-hairpin with three flexibly disordered loops extending from the central b-sheet. A homology search with the software DALI identified two Protein Data Bank deposits with Z-scores > 8, where both of these proteins have less than 8% sequence identity relative to NP_888769.1, and one has been functionally annotated as a lambda phage tail terminator protein. A sequence-homology analysis then confirmed that NP_888769.1 represents the first three-dimensional structural representative of a new protein family that was previously predicted by the Joint Center for Structural Genomics, which includes so far about 20 prophage proteins encoded in bacterial genomes.

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The X-Ray Crystal Structure of the Phage λ Tail Terminator Protein Reveals the Biologically Relevant Hexameric Ring Structure and Demonstrates a Conserved Mechanism of Tail Termination among Diverse Long-Tailed Phages

Cited by 57 publications

References 53 publications

Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage‐related protein family PF13554

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