Conservation of the capsid structure in tailed dsDNA bacteriophages

The pseudoatomic structure of φ29

Marc Morais, Kyung Choi, Jaya S. Koti, Paul R. Chipman, Dwight L. Anderson, Michael G. Rossmann

Research output: Contribution to journalArticle

142 Citations (Scopus)

Abstract

Bacteriophage φ29 is one of the smallest and simplest known dsDNA phages, making it amenable to structural investigations. The three-dimensional structure of a fiberless, isometric variant has been determined to 7.9 Å resolution by cryo-electron microscopy (cryo-EM), allowing the identification of α helices and β sheets. Their arrangement indicates that the folds of the φ29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the φ29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric φ29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead φ29 particles at resolutions of 8.7 Å and 12.7 Å, respectively. Thus, φ29 joins the growing number of phages that utilize the HK97 capsid structure, suggesting that this protein fold may be as prevalent in capsids of dsDNA phages as the jelly roll fold is in eukaryotic viruses.

Original languageEnglish (US)
Pages (from-to)149-159
Number of pages11
JournalMolecular Cell
Volume18
Issue number2
DOIs
StatePublished - Apr 15 2005
Externally publishedYes

Fingerprint

Capsid
Bacteriophages
Cryoelectron Microscopy
Phosmet
Capsid Proteins
Proteins
Viruses

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Conservation of the capsid structure in tailed dsDNA bacteriophages : The pseudoatomic structure of φ29. / Morais, Marc; Choi, Kyung; Koti, Jaya S.; Chipman, Paul R.; Anderson, Dwight L.; Rossmann, Michael G.

In: Molecular Cell, Vol. 18, No. 2, 15.04.2005, p. 149-159.

Research output: Contribution to journalArticle

Morais, Marc ; Choi, Kyung ; Koti, Jaya S. ; Chipman, Paul R. ; Anderson, Dwight L. ; Rossmann, Michael G. / Conservation of the capsid structure in tailed dsDNA bacteriophages : The pseudoatomic structure of φ29. In: Molecular Cell. 2005 ; Vol. 18, No. 2. pp. 149-159.
@article{4aa97884385e477f9f31c7e677066744,
title = "Conservation of the capsid structure in tailed dsDNA bacteriophages: The pseudoatomic structure of φ29",
abstract = "Bacteriophage φ29 is one of the smallest and simplest known dsDNA phages, making it amenable to structural investigations. The three-dimensional structure of a fiberless, isometric variant has been determined to 7.9 {\AA} resolution by cryo-electron microscopy (cryo-EM), allowing the identification of α helices and β sheets. Their arrangement indicates that the folds of the φ29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the φ29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric φ29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead φ29 particles at resolutions of 8.7 {\AA} and 12.7 {\AA}, respectively. Thus, φ29 joins the growing number of phages that utilize the HK97 capsid structure, suggesting that this protein fold may be as prevalent in capsids of dsDNA phages as the jelly roll fold is in eukaryotic viruses.",
author = "Marc Morais and Kyung Choi and Koti, {Jaya S.} and Chipman, {Paul R.} and Anderson, {Dwight L.} and Rossmann, {Michael G.}",
year = "2005",
month = "4",
day = "15",
doi = "10.1016/j.molcel.2005.03.013",
language = "English (US)",
volume = "18",
pages = "149--159",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Conservation of the capsid structure in tailed dsDNA bacteriophages

T2 - The pseudoatomic structure of φ29

AU - Morais, Marc

AU - Choi, Kyung

AU - Koti, Jaya S.

AU - Chipman, Paul R.

AU - Anderson, Dwight L.

AU - Rossmann, Michael G.

PY - 2005/4/15

Y1 - 2005/4/15

N2 - Bacteriophage φ29 is one of the smallest and simplest known dsDNA phages, making it amenable to structural investigations. The three-dimensional structure of a fiberless, isometric variant has been determined to 7.9 Å resolution by cryo-electron microscopy (cryo-EM), allowing the identification of α helices and β sheets. Their arrangement indicates that the folds of the φ29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the φ29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric φ29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead φ29 particles at resolutions of 8.7 Å and 12.7 Å, respectively. Thus, φ29 joins the growing number of phages that utilize the HK97 capsid structure, suggesting that this protein fold may be as prevalent in capsids of dsDNA phages as the jelly roll fold is in eukaryotic viruses.

AB - Bacteriophage φ29 is one of the smallest and simplest known dsDNA phages, making it amenable to structural investigations. The three-dimensional structure of a fiberless, isometric variant has been determined to 7.9 Å resolution by cryo-electron microscopy (cryo-EM), allowing the identification of α helices and β sheets. Their arrangement indicates that the folds of the φ29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the φ29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric φ29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead φ29 particles at resolutions of 8.7 Å and 12.7 Å, respectively. Thus, φ29 joins the growing number of phages that utilize the HK97 capsid structure, suggesting that this protein fold may be as prevalent in capsids of dsDNA phages as the jelly roll fold is in eukaryotic viruses.

UR - http://www.scopus.com/inward/record.url?scp=17044395121&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17044395121&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2005.03.013

DO - 10.1016/j.molcel.2005.03.013

M3 - Article

VL - 18

SP - 149

EP - 159

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 2

ER -