The Structure of the Receptor-binding Domain of the Bacteriophage T4 Short Tail Fibre Reveals a Knitted Trimeric Metal-binding Fold

Thomassen, E.A.J.; Gielen, Gerrit; Schutz, M.M.; Schoehn, Guy; Abrahams, Jan Pieter; Miller, Stefan; Raaij, Mark J. van

doi:10.1016/s0022-2836(03)00755-1

Cited by 103 publications

(90 citation statements)

References 48 publications

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“…In the core of the needle domain, hydrophobic and hydrophilic regions alternate, with the latter forming the metal-binding sites. The seven iron ions are coordinated octahedrally by the Nϵ atoms of two histidine residues from each chain, in a similar fashion to the zinc ion in the structure of gp12 (25). Iron ions 1, 5, and 7 are bound by the His-883/His-885, His-915/His-917, and His-929/His-931 doublets, respectively, whereas the His-966/His-968, His-980/His-982, His-989/His-991, and His-998/His-1000 pairs from the returning strand coordinate iron ions 6, 4, 3, and 2 (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…Similarity extends to the intertwined region adjacent to the collar domain and the first metal-binding site. His-885 and His-887 superpose well onto His-445 and His-447 of gp12, respectively, although gp12 binds a zinc ion instead of iron (25,28). Gene product 10 (29) also exhibits significant structural homology to gp37, and 87 C-alpha atoms can be superposed with an rmsd of 4.8 Å.…”

Section: Resultsmentioning

confidence: 98%

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

Bartual

Otero²,

Garcia-Doval³

et al. 2010

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

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167

195

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Bacteriophages are the most numerous organisms in the biosphere. In spite of their biological significance and the spectrum of potential applications, little high-resolution structural detail is available on their receptor-binding fibers. Here we present the crystal structure of the receptor-binding tip of the bacteriophage T4 long tail fiber, which is highly homologous to the tip of the bacteriophage lambda side tail fibers. This structure reveals an unusual elongated sixstranded antiparallel beta-strand needle domain containing seven iron ions coordinated by histidine residues arranged colinearly along the core of the biological unit. At the end of the tip, the three chains intertwine forming a broader head domain, which contains the putative receptor interaction site. The structure reveals a previously unknown beta-structured fibrous fold, provides insights into the remarkable stability of the fiber, and suggests a framework for mutations to expand or modulate receptor-binding specificity.gene product 37 | host cell attachment | octahedral coordination | viral fibers | X-ray crystallography

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 98%

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

Bartual

Otero²,

Garcia-Doval³

et al. 2010

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

Self Cite

167

195

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show abstract

“…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%

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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“…Molecular mechanisms deduced from genomic information on phage-host interactions, no matter how general or specific, could be useful for establishing long-lasting phage biocontrol systems. These include, for example, general interactions (Comeau & Krisch, 2007), restriction/antirestriction systems (Tock & Dryden, 2005;Hoskisson & Smith, 2007), and phage receptor/host adsorption interactions (Goldberg et al, 1994;Tetart et al, 1998;Thomassen et al, 2003).…”

Section: Future Prospectsmentioning

confidence: 99%

Bacteriophages of Ralstonia solanacearum: Their Diversity and Utilization as Biocontrol Agents in Agriculture

Yamada¹

2012

Bacteriophages

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The Structure of the Receptor-binding Domain of the Bacteriophage T4 Short Tail Fibre Reveals a Knitted Trimeric Metal-binding Fold

Cited by 103 publications

References 48 publications

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

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

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

Bacteriophages of Ralstonia solanacearum: Their Diversity and Utilization as Biocontrol Agents in Agriculture

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