Abstract. The product of gene 9 (gp9) of Salmonella typhimurium bacteriophage P22 is a multifunctional structural protein. This protein is both a specific glycosidase which imparts the adsorption characteristics of the phage for its host and a protein which participates in a specific assembly reaction during phage morphogenesis.

Jun 12, · Bacteriophage tails. (A) The crystal structure of a monomer of T5 pb6 (5NGJ). The extra immunoglobulin domain is coloured yellow. (B) A slice of the combined EM map of T5 (EMD-3692) showing the fold symmetry of the tail. (C) The crystal structure of the N-terminal domain of the P22 TP gpV (2K4Q). (D) Cryo-EM map of SPP1 tails (gp17.1).

The portal channel is a key component in the life cycle of bacteriophages and herpesviruses. The bacteriophage P22 portal is a 1 megadalton dodecameric oligomer of gp1 that plays key roles in capsid assembly, DNA packaging, assembly of the infection machinery, and DNA ejection. The portal is the nucleation site for the assembly of 39 additional subunits generated from multiple copies of four

Abstract. The product of gene 9 (gp9) of Salmonella typhimurium bacteriophage P22 is a multifunctional structural protein. This protein is both a specific glycosidase which imparts the adsorption characteristics of the phage for its host and a protein which participates in a

A complex structure known as the "portal" connects the tail and the capsid, and is required both to load the capsid with DNA (or RNA) and to mediate its injection into the host bacterium. P22, which belongs to the Podoviridae family of short-tailed phages, has a large portal vertex structure consisting of 51 polypeptide chains of 5 different types.

Three-dimensional structure of the bacteriophage P22 tail machine. The EMBO Journal 2005, 24 Three-dimensional structure of T3 connector purified from

Structure and functions of the bacteriophage P22 tail protein. Berget PB, Poteete AR. The product of gene 9 (gp9) of Salmonella typhimurium bacteriophage P22 is a multifunctional structural protein. This protein is both a specific glycosidase which imparts the adsorption characteristics of the phage for its host and a protein which participates in a specific assembly reaction during phage morphogenesis.

Bacteriophage P22 tail machine - isolated from bacteriophage P22: ID: EM-1119: Citation: Three-dimensional structure of the bacteriophage P22 tail machine: Family: T-Number:

Bacteriophage P22 infects Salmonella enterica by injecting its genetic material through the cell envelope. During infection, a specialized tail needle, gp26, is injected into the host, likely piercing a hole in the host cell envelope. The 2.1-Å cryst

The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are

surface of the coiled-coil in the P22 structure to form what may be the site through which the needle binds in the tail channel to form the plug. Although they are homologous in their N-terminal virion-binding domain, P22 and Sf6 have completely different domains at their C-termini; the biological reason for this is not known [26,27,28].

12/15 · Here, the atomic structure of a virally encoded, cell-wall-spanning, DNA-translocating conduit from bacteriophage ΦX174 is described. This paper presents the first atomic structure

The bacteriophage P22 portal is a 1 megadalton dodecameric oligomer of gp1 that plays key roles in capsid assembly, DNA packaging, assembly of the infection machinery, and DNA ejection. The portal is the nucleation site for the assembly of 39 additional subunits generated from multiple copies of four gene products (gp4, gp10, gp9, and gp26

P22 is a member of the Podoviridae, with a 57 nm icosahedral head, a short tail, a sort of baseplate made up of six trimers of the tailspike protein, and a single fiber extending from the middle of the baseplate. The 41724 bp genome includes 64 genes and unidentified open reading frames (ORFs).

Bacterial viruses of the P22-like family encode a specialized tail needle essential for genome stabilization after DNA packaging and implicated in Gram-negative cell envelope penetration. The atomic structure of P22 tail needle (gp26) crystallized at acidic pH reveals a slender fiber containing an N-terminal “trimer of hairpins” tip. Although the length and composition of tail needles vary

Jan 10, · Structure of Bacteriophage Each bacteriophage consists of the nucleic acid genome that enclosed in a protein coat, known as a capsid or surrounded by a lipid membrane called an envelope. Its capsid consists of repeating protein subunits known as protomers and it is important in packaging the phage genome and transfer of genome into a host cell.

Morphology, classification and relatives. P22 shares many similarities in genetic structure and regulation with bacteriophage λ. It is a temperate double stranded DNA phage as well as a lambdoid phage since it carries control of gene expression regions and early operons similar to those of bacteriophage λ.

A complex structure known as the "portal" connects the tail and the capsid, and is required both to load the capsid with DNA (or RNA) and to mediate its injection into the host bacterium. P22, which belongs to the Podoviridae family of short-tailed phages, has a large portal vertex structure consisting of 51 polypeptide chains of 5 different types.

Berget PB, Poteete AR. Structure and functions of the bacteriophage P22 tail protein. J Virol. 1980 Apr; 34 (1):234-243. [PMC free article] Iwashita S, Kanegasaki S. Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22. Biochem Biophys Res Commun. 1973 Nov 16; 55 (2):403-409.

Mature particles of bacteriophage ϕ29 consist of a 33-MDa complex formed by over 450 subunits, assembled into a head and a short tail. Here, Xu et al. report the near-atomic structures of the

Structure Article The P22 Tail Machine at Subnanometer Resolution Reveals the Architecture of an Infection Conduit Gabriel C. Lander,1,2 Reza Khayat,2 Rui Li,3 Peter E. Prevelige,3 Clinton S. Potter,1 Bridget Carragher,1 and John E. Johnson2,* 1National Resource for Automated Molecular Microscopy, The Scripps Institute, La Jolla, CA 92037, USA 2Department of Molecular Biology, The Scripps