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New page: left|200px<br /><applet load="1dnv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dnv, resolution 3.6Å" /> '''PARVOVIRUS (DENSOVIRU...
 
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[[Image:1dnv.jpg|left|200px]]<br /><applet load="1dnv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dnv.jpg|left|200px]]<br /><applet load="1dnv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dnv, resolution 3.6&Aring;" />
caption="1dnv, resolution 3.6&Aring;" />
'''PARVOVIRUS (DENSOVIRUS) FROM GALLERIA MELLONELLA'''<br />
'''PARVOVIRUS (DENSOVIRUS) FROM GALLERIA MELLONELLA'''<br />


==Overview==
==Overview==
BACKGROUND: Parvoviruses infect vertebrates, insects and crustaceans. Many, arthropod parvoviruses (densoviruses) are highly pathogenic and kill, approximately 90% of the host larvae within days, making them potentially, effective as selective pesticides. Improved understanding of densoviral, structure and function is therefore desirable. There are four different, initiation sites for translation of the densovirus capsid protein mRNA, giving rise to the viral proteins VP1 to VP4. Sixty copies of the common, C-terminal domain make up the ordered part of the icosahedral capsid., RESULTS: The Galleria mellonella densovirus (GMDNV) capsid protein, consists of a core beta-barrel motif, similar to that found in many other, viral capsid proteins. The structure most closely resembles that of the, vertebrate parvoviruses, but it has diverged beyond recognition in many of, the long loop regions that constitute the surface features and, intersubunit contacts. The N termini of twofold-related subunits have, swapped their positions relative to those of the vertebrate parvoviruses., Unlike in the vertebrate parvoviruses, in GmDNV there is no continuous, electron density in the channels running along the fivefold axes of the, virus. Electron density corresponding to some of the single-stranded DNA, genome is visible in the crystal structure, but it is not as well defined, as in the vertebrate parvoviruses. CONCLUSIONS: The sequence of the, glycine-rich motif, which occupies each of the channels along the fivefold, axes in vertebrate viruses, is conserved between mammalian and insect, parvoviruses. This motif may serve to externalize the N-terminal region of, the single VP1 subunit per particle. The domain swapping of the N termini, between insect and vertebrate parvoviruses may have the effect of, increasing capsid stability in GmDNV.
BACKGROUND: Parvoviruses infect vertebrates, insects and crustaceans. Many arthropod parvoviruses (densoviruses) are highly pathogenic and kill approximately 90% of the host larvae within days, making them potentially effective as selective pesticides. Improved understanding of densoviral structure and function is therefore desirable. There are four different initiation sites for translation of the densovirus capsid protein mRNA, giving rise to the viral proteins VP1 to VP4. Sixty copies of the common, C-terminal domain make up the ordered part of the icosahedral capsid. RESULTS: The Galleria mellonella densovirus (GMDNV) capsid protein consists of a core beta-barrel motif, similar to that found in many other viral capsid proteins. The structure most closely resembles that of the vertebrate parvoviruses, but it has diverged beyond recognition in many of the long loop regions that constitute the surface features and intersubunit contacts. The N termini of twofold-related subunits have swapped their positions relative to those of the vertebrate parvoviruses. Unlike in the vertebrate parvoviruses, in GmDNV there is no continuous electron density in the channels running along the fivefold axes of the virus. Electron density corresponding to some of the single-stranded DNA genome is visible in the crystal structure, but it is not as well defined as in the vertebrate parvoviruses. CONCLUSIONS: The sequence of the glycine-rich motif, which occupies each of the channels along the fivefold axes in vertebrate viruses, is conserved between mammalian and insect parvoviruses. This motif may serve to externalize the N-terminal region of the single VP1 subunit per particle. The domain swapping of the N termini between insect and vertebrate parvoviruses may have the effect of increasing capsid stability in GmDNV.


==About this Structure==
==About this Structure==
1DNV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Galleria_mellonella_densovirus Galleria mellonella densovirus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DNV OCA].  
1DNV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Galleria_mellonella_densovirus Galleria mellonella densovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DNV OCA].  


==Reference==
==Reference==
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[[Category: Galleria mellonella densovirus]]
[[Category: Galleria mellonella densovirus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baker, T.S.]]
[[Category: Baker, T S.]]
[[Category: Chipmann, P.R.]]
[[Category: Chipmann, P R.]]
[[Category: Rossmann, M.G.]]
[[Category: Rossmann, M G.]]
[[Category: Simpson, A.A.]]
[[Category: Simpson, A A.]]
[[Category: Tijssen, P.]]
[[Category: Tijssen, P.]]
[[Category: capsid protein]]
[[Category: capsid protein]]
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[[Category: viral capsid]]
[[Category: viral capsid]]


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