Unknown

Dataset Information

0

Structural conservation of the myoviridae phage tail sheath protein fold.


ABSTRACT: Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 Å resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 Å resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4.

SUBMITTER: Aksyuk AA 

PROVIDER: S-EPMC3256926 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural conservation of the myoviridae phage tail sheath protein fold.

Aksyuk Anastasia A AA   Kurochkina Lidia P LP   Fokine Andrei A   Forouhar Farhad F   Mesyanzhinov Vadim V VV   Tong Liang L   Rossmann Michael G MG  

Structure (London, England : 1993) 20111201 12


Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 Å resolution. Furthermore, crystal structur  ...[more]

Similar Datasets

| S-EPMC5862860 | biostudies-literature
| S-EPMC8570332 | biostudies-literature
| S-EPMC8618960 | biostudies-literature
| S-EPMC7431101 | biostudies-literature
| S-EPMC4460457 | biostudies-literature
| S-EPMC2760360 | biostudies-literature
| S-EPMC3622015 | biostudies-literature
| S-EPMC2142618 | biostudies-other
| S-EPMC3675071 | biostudies-literature