Structure of the bacteriophage T4 long tail fiber receptor-binding tip

Bartual, S.G.; Otero, José M.; Garcia-Doval, Carmela; Llamas-Saíz, Antonio L.; Kahn, Richard; Fox, Gavin C.; Raaij, Mark J. van

doi:10.1073/pnas.1011218107

Cited by 167 publications

(200 citation statements)

References 49 publications

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“…The receptor-binding proteins of lactococcus phages p2 and TP901-1 also have a similar C-terminal domain attached to a short β-helical stalk (36,37). The bacteriophage T4 short tail-fiber (gp12) and long tailfiber (gp37) C-terminal domains have different folds, consisting of three intertwined monomers rather than composed of individually folded monomeric domains (21,38), and T4 fibritin (gpwac) and the phage P22 cell-penetrating needle (gp26) have a much smaller trimerisation domain (39,40).…”

Section: Discussionmentioning

confidence: 99%

“…The tail-spike of the podovirus P22 has been studied extensively in terms of carbohydrate binding, hydrolysis, folding, and assembly (17,18). Much is also known about assembly and function of the complex fibers of the myovirus T4 (19)(20)(21). Siphoviruses like T5 and λ contain less-studied side tail fibers (22, 23) which, like the T4 fibers, do not exhibit receptor-hydrolysis activity.…”

Section: Discussionmentioning

confidence: 99%

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Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

Garcia-Doval

Raaij

2012

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

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104

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The six bacteriophage T7 tail fibers, homo-trimers of gene product 17, are thought to be responsible for the first specific, albeit reversible, attachment to Escherichia coli lipopolysaccharide. The protein trimer forms kinked fibers comprised of an amino-terminal tail-attachment domain, a slender shaft, and a carboxyl-terminal domain composed of several nodules. Previously, we expressed, purified, and crystallized a carboxyl-terminal fragment comprising residues 371-553. Here, we report the structure of this protein trimer, solved using anomalous diffraction and refined at 2 Å resolution. Amino acids 371-447 form a tapered pyramid with a triangular cross-section composed of interlocked β-sheets from each of the three chains. The triangular pyramid domain has three α-helices at its narrow end, which are connected to a carboxyl-terminal three-blade β-propeller tip domain by flexible loops. The monomers of this tip domain each contain an eight-stranded β-sandwich. The exact topology of the β-sandwich fold is novel, but similar to that of knob domains of other viral fibers and the phage Sf6 needle. Several host-range change mutants have been mapped to loops located on the top of this tip domain, suggesting that this surface of the tip domain interacts with receptors on the cell surface.bacterial viruses | caudovirales | crystallography | infection | Podoviridae B acteriophages (bacterial viruses or phages) are important biological model systems and, because of the high specificity for their host bacteria, have found application in phage typing, food security, and phage therapy (1). Escherichia coli phage T7 is a member of the Podoviridae family of the Caudovirales (tailed phages) order (2). T7 is composed of an icosahedral capsid with a 20-nm short tail at one of the vertices (3, 4). The capsid is formed by the shell protein gene product (gp) 10 and encloses a DNA of 40 kb. A cylindrical structure composed of gp14, gp15, and gp16 is present inside the capsid (5), attached to the special vertex formed by the connector, a circular dodecamer of gp8 (6). Gp11 and gp12 form the tail; gp13, gp6.7, and gp7.3 have also been shown to be part of the virion and to be necessary for infection, although their location has not been established (7,8). Although extensive electron microscopy studies have been performed on phage T7 (3-6, 9), crystallographic studies have so far been limited to its nonstructural proteins.The main portion of the tail is composed of gp12, a large protein of which six copies are present (10); the small gp11 protein is also located in the tail (5). Attached to the tail are six fibers, each containing three copies of the gp17 protein. T7 tail fibers are elongated homo-trimers, which are responsible for initial, reversible, host cell recognition. A second, irreversible, decisionmaking interaction with the bacterial membrane is presumably mediated by one or more of the tail-tube proteins. DNA transfer into the host is then mediated by an extension formed by gp14-16 (7, 8, 11). Previously, we have reported t...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

Garcia-Doval

Raaij

2012

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

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104

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“…The long tail fibers, with a length of ~1450 Å, bind reversibly to the E.coli lipopolysaccharide (LPS) and/or OmpC molecules, and serve for primary host recognition. 151 Upon binding of the long tail fibers a signal is send to the baseplate causing the 6 short tail fibers to extend and bind irreversibly to the LPS. On attachment, the baseplate conformation switches from the dome-shaped to the star-shaped which, in turn, triggers the contraction of the tail sheath.…”

Section: Structure Of the Phage Tailsmentioning

confidence: 99%

Molecular architecture of tailed double-stranded DNA phages

2014

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“…4A) (14). The bacteriophage T4 tail needle fiber (23), the T4 long tail fiber (24), and the adenovirus fiber (25) structures each represent a different β-structured fold (Fig. 4A).…”

Section: Structural Comparisons With Other Fiber Structures In Virusesmentioning

confidence: 99%

Structure of bacteriophage ϕ 29 head fibers has a supercoiled triple repeating helix-turn-helix motif

Xiang

Rossmann²

2011

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

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The tailed bacteriophage ϕ29 capsid is decorated with 55 fibers attached to quasi-3-fold symmetry positions. Each fiber is a homotrimer of gene product 8.5 (gp8.5) and consists of two major structural parts, a pseudohexagonal base and a protruding fibrous portion that is about 110 Å in length. The crystal structure of the C-terminal fibrous portion (residues 112-280) has been determined to a resolution of 1.6 Å. The structure is about 150 Å long and shows three distinct structural domains designated as head, neck, and stem. The stem region is a unique three-stranded helix-turn-helix supercoil that has not previously been described. When fitted into a cryoelectron microscope reconstruction of the virus, the head structure corresponded to a disconnected density at the distal end of the fiber and the neck structure was located in weak density connecting it to the fiber. Thin section studies of Bacillus subtilis cells infected with fibered or fiberless ϕ29 suggest that the fibers might enhance the attachment of the virions onto the host cell wall.infection | phi29 | supersecondary structure | X-ray crystallography

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Structure of the bacteriophage T4 long tail fiber receptor-binding tip

Cited by 167 publications

References 49 publications

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

Molecular architecture of tailed double-stranded DNA phages

Structure of bacteriophage ϕ 29 head fibers has a supercoiled triple repeating helix-turn-helix motif

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