1yxn
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(New page: 200px<br /><applet load="1yxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxn" /> '''Pseudo-atomic model of a fiberless isometric...)
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Revision as of 02:31, 25 November 2007
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Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29
Overview
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.
About this Structure
1YXN is a Protein complex structure of sequences from Vibrio phage f237. Full crystallographic information is available from OCA.
Reference
Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29., Morais MC, Choi KH, Koti JS, Chipman PR, Anderson DL, Rossmann MG, Mol Cell. 2005 Apr 15;18(2):149-59. PMID:15837419
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