The<i>Wac</i>Gene Product of Bacteriophage T4 Contains Coiled-Coil Structural Patterns

Sobolev, Boris N.; Mesyanzhinov, Vadim V.

doi:10.1080/07391102.1991.10507859

Cited by 10 publications

(10 citation statements)

References 27 publications

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“…The heptad positions shown in the T4 gpwac sequence are those proposed by Sobolev and Mesyanzhinov (33) with the corrections of Tao et al (36). The loops of the gpwac of bacteriophage T4 (33,36) distant (Ͻ80% amino acid identity) T4-type phages had unrelated C-terminal domains (Fig. 3).…”

Section: Structure and Function Of The Wac Protein Of Phage T4supporting

confidence: 54%

“…2). Furthermore, the positions of the interruptions in this periodicity can usually be aligned to the loop positions predicted in the T4 gpwac (33,36). In the gpwac of phage 42 the T4 loop 11 is deleted (Fig.…”

Section: Structure and Function Of The Wac Protein Of Phage T4mentioning

confidence: 96%

“…Both LTFs and short tail fibers have a similar trimeric parallel ␤-helical protein structure (26,39). However, the 486-amino-acid (aa) T4 gpwac polypeptide trimerizes into a coiled-coil ␣-helical structure that is flanked by small N-and C-terminal globular domains (14,28,33). It is the N-terminal 50-aa domain of T4 gpwac that binds to the neck of the phage, whereas the 30-aa C-terminal domain of the protein (the "foldon") is essential for the initiation of trimerization and the correct folding of the polypeptide chains in the fiber (14,23).…”

mentioning

confidence: 99%

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gpwac of the T4-Type Bacteriophages: Structure, Function, and Evolution of a Segmented Coiled-Coil Protein That Controls Viral Infectivity

et al. 2005

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The wac gene product (gpwac) or fibritin of bacteriophage T4 forms the six fibers that radiate from the phage neck. During phage morphogenesis these whiskers bind the long tail fibers (LTFs) and facilitate their attachment to the phage baseplate. After the cell lysis, the gpwac fibers function as part of an environmental sensing device that retains the LTFs in a retracted configuration and thus prevents phage adsorption in unfavorable conditions. A comparative analysis of the sequences of 5 wac gene orthologs from various T4-type phages reveals that the ϳ50-amino-acid N-terminal domain is the only highly conserved segment of the protein. This sequence conservation is probably a direct consequence of the domain's strong and specific interactions with the neck proteins. The sequence of the central fibrous region of gpwac is highly plastic, with only the heptad periodicity of the coiled-coil structure being conserved. In the various gpwac sequences, the small C-terminal domain essential for initiation of the folding of T4 gpwac is replaced by unrelated sequences of unknown origin. When a distant T4-type phage has a novel C-terminal gpwac sequence, the phage's gp36 sequence that is located at the knee joint of the LTF invariably has a novel domain in its C terminus as well. The covariance of these two sequences is compatible with genetic data suggesting that the C termini of gpwac and gp36 engage in a protein-protein interaction that controls phage infectivity. These results add to the limited evidence for domain swapping in the evolution of phage structural proteins.

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Section: Structure and Function Of The Wac Protein Of Phage T4supporting

confidence: 54%

Section: Structure and Function Of The Wac Protein Of Phage T4mentioning

confidence: 96%

mentioning

confidence: 99%

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gpwac of the T4-Type Bacteriophages: Structure, Function, and Evolution of a Segmented Coiled-Coil Protein That Controls Viral Infectivity

et al. 2005

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“…The sequence of the gpwac polypeptide chain of 487 residues is composed of heptad repeats (a b c d e f g) n , with the a and d positions preferentially occupied by apo lar residues and the e and g positions often occupied by charged residues [92]. Such a motif, a characteristic fea ture of α helical coiled coils proteins, is widely distrib uted [93].…”

Section: The Structures Of Phage Fibersmentioning

confidence: 99%

Molecular architecture of bacteriophage T4

Mesyanzhinov

Leiman

Kostyuchenko

et al. 2004

Biochemistry (Moscow)

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In studying bacteriophage T4--one of the basic models of molecular biology for several decades--there has come a Renaissance, and this virus is now actively used as object of structural biology. The structures of six proteins of the phage particle have recently been determined at atomic resolution by X-ray crystallography. Three-dimensional reconstruction of the infection device--one of the most complex multiprotein components--has been developed on the basis of cryo-electron microscopy images. The further study of bacteriophage T4 structure will allow a better understanding of the regulation of protein folding, assembly of biological structures, and also mechanisms of functioning of the complex biological molecular machines.

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“…5 Sequence analysis of fibritin reveals a major region (, 80% of the entire sequence) which contains the heptad repeat pattern (abcdefg) n , where a and d are preferably occupied by apolar residues. 10,11 Such a motif is characteristic of an a-helical coiled-coil structure. 12 In fibritin the heptad pattern is interrupted in several places, which suggests the existence of 13 coiled-coil "segments" connected by 12 linker regions ( Figure 2).…”

Section: Introductionmentioning

confidence: 99%