1YXN

Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29

Summary for 1YXN

• Entry DOI: 10.2210/pdb1yxn/pdb
• Related: 1F00 1OHG
• EMDB information: 1116 1120
• Descriptor: Major head protein (1 entity in total)
• Functional Keywords: phi29, capsid, icosahedral virus capsid, hk97 fold, phage, bacterial immuno-globulin, big2, icosahedral virus, virus
• Biological source: Bacillus phage phi29
• Total number of polymer chains: 3
• Total formula weight: 91967.00

Authors

Morais, M.C.,Choi, K.H.,Koti, J.S.,Chipman, P.R.,Anderson, D.L.,Rossmann, M.G. (deposition date: 2005-02-22, release date: 2005-04-26, Last modification date: 2024-02-14)

Primary citation

Morais, M.C.,Choi, K.H.,Koti, J.S.,Chipman, P.R.,Anderson, D.L.,Rossmann, M.G.
Conservation of the Capsid Structure in Tailed dsDNA Bacteriophages: the Pseudoatomic Structure of phi29
Mol.Cell, 18:149-159, 2005

PubMed Abstract: Bacteriophage phi29 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 A resolution by cryo-electron microscopy (cryo-EM), allowing the identification of alpha helices and beta sheets. Their arrangement indicates that the folds of the phi29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the phi29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric phi29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead phi29 particles at resolutions of 8.7 A and 12.7 A, respectively. Thus, phi29 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.

PubMed: 15837419
DOI: 10.1016/j.molcel.2005.03.013

Experimental method

ELECTRON MICROSCOPY (7.9 Å)