About: Three-dimensional structure of the bacteriophage P22 tail machine

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Three-dimensional structure of the bacteriophage P22 tail machine
Creator	Cingolani, Gino Tang, Liang Johnson, John Marion, William Prevelige, Peter
source	Medline; PMC
abstract	The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. 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 organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation.
has issue date	2005-06-02(xsd:dateTime)
bibo:doi	10.1038/sj.emboj.7600695
bibo:pmid	15933718
has license	green-oa
sha1sum (hex)	b1bb2403837df337ef7fa75a252c9eba2be6e29a
schema:url	https://doi.org/10.1038/sj.emboj.7600695
resource representing a document's title	Three-dimensional structure of the bacteriophage P22 tail machine
has PubMed Central identifier	PMC1150889
has PubMed identifier	15933718
schema:publication	The EMBO Journal
resource representing a document's body	covid:b1bb2403837df337ef7fa75a252c9eba2be6e29a#body_text
is schema:about of	named entity 'types' named entity 'three-fold' named entity 'twelve-' covid:arg/b1bb2403837df337ef7fa75a252c9eba2be6e29a named entity 'THE EMBO JOURNAL' named entity 'electron cryo-microscopy' named entity 'P22' named entity 'Three-dimensional' named entity 'EMBO' named entity 'translocation' named entity 'polypeptides' named entity 'electron cryo-microscopy' named entity 'bacteriophage' named entity 'phage' named entity 'gp10' named entity 'Maurides' named entity 'E. coli' named entity 'receptor' named entity 'three-dimensional reconstruction' named entity 'dodecameric' named entity 'gp10' named entity 'SPP1' named entity 'phages' named entity '6xHis' named entity 'cytoplasm' named entity 'monomer' named entity 'protein' named entity 'liquid nitrogen' named entity 'cryoEM' named entity 'ligated' named entity 'dsDNA' named entity 'kDa' named entity 'CryoEM' named entity 'Fourier shell correlation' named entity 'protein' named entity 'Philips' named entity 'phage' named entity 'gp10' named entity 'CryoEM' named entity 'coiled coil' named entity 'Caudovirales' named entity 'cryoEM' named entity 'procapsid' named entity 'gp10' named entity 'capsid' named entity 'Salmonella enterica' named entity 'sedimentation equilibrium' named entity 'gp9' named entity 'cryoEM' named entity 'trimer' named entity 'Fourier shell correlation' named entity 'X-ray' named entity 'electron micrographs' named entity 'trimer' named entity 'C-terminal' named entity 'lysis buffer' named entity 'structural motif' named entity 'conformational change' named entity 'dsDNA' named entity 'hexamer' named entity 'lysate' named entity 'ethane' named entity 'dodecameric' named entity 'gp16' named entity 'gp10' named entity 'phage' named entity 'bacteriophages' named entity 'infection' named entity 'Molineux' named entity 'procapsid' named entity 'gp10' named entity 'Pharmacia' named entity 'phage' named entity 'hexameric' named entity 'micrographs' named entity 'N-terminal domain' named entity 'P22'

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