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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'''Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29'''<br />
'''Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YXN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YXN OCA].
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1YXN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXN OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Vibrio phage f237]]
[[Category: Vibrio phage f237]]
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[[Category: Anderson, D.L.]]
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[[Category: Anderson, D L.]]
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[[Category: Chipman, P.R.]]
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[[Category: Chipman, P R.]]
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[[Category: Choi, K.H.]]
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[[Category: Choi, K H.]]
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[[Category: Koti, J.S.]]
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[[Category: Koti, J S.]]
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[[Category: Morais, M.C.]]
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[[Category: Morais, M C.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
[[Category: bacterial immuno-globulin]]
[[Category: bacterial immuno-globulin]]
[[Category: big2]]
[[Category: big2]]
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[[Category: phi29]]
[[Category: phi29]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:38:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:10 2008''

Revision as of 14:10, 21 February 2008


1yxn

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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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