1yq5
From Proteopedia
(New page: 200px<br /><applet load="1yq5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yq5, resolution 2.0Å" /> '''PRD1 vertex protein P...) |
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| - | [[Image:1yq5.gif|left|200px]]<br /><applet load="1yq5" size=" | + | [[Image:1yq5.gif|left|200px]]<br /><applet load="1yq5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yq5, resolution 2.0Å" /> | caption="1yq5, resolution 2.0Å" /> | ||
'''PRD1 vertex protein P5'''<br /> | '''PRD1 vertex protein P5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Comparisons of bacteriophage PRD1 and adenovirus protein structures and | + | Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion. |
==About this Structure== | ==About this Structure== | ||
| - | 1YQ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1]. Full crystallographic information is available from [http:// | + | 1YQ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQ5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Enterobacteria phage prd1]] | [[Category: Enterobacteria phage prd1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bamford, D | + | [[Category: Bamford, D H.]] |
[[Category: Goldman, A.]] | [[Category: Goldman, A.]] | ||
| - | [[Category: Huiskonen, J | + | [[Category: Huiskonen, J T.]] |
| - | [[Category: Merckel, M | + | [[Category: Merckel, M C.]] |
[[Category: Tuma, R.]] | [[Category: Tuma, R.]] | ||
[[Category: beta-jelly-roll]] | [[Category: beta-jelly-roll]] | ||
[[Category: beta-spiral]] | [[Category: beta-spiral]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:55 2008'' |
Revision as of 14:07, 21 February 2008
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PRD1 vertex protein P5
Overview
Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion.
About this Structure
1YQ5 is a Single protein structure of sequence from Enterobacteria phage prd1. Full crystallographic information is available from OCA.
Reference
The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture., Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R, Mol Cell. 2005 Apr 15;18(2):161-70. PMID:15837420
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