1f2n: Difference between revisions

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[[Image:1f2n.jpg|left|200px]]<br /><applet load="1f2n" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1f2n.jpg|left|200px]]<br /><applet load="1f2n" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1f2n, resolution 2.8Å" />

'''RICE YELLOW MOTTLE VIRUS'''<br />

==Overview==

BACKGROUND: Rice yellow mottle virus (RYMV) is a major pathogen that, dramatically reduces rice production in many African countries. RYMV, belongs to the genus sobemovirus, one group of plant viruses with, icosahedral capsids and single-stranded, positive-sense RNA genomes., RESULTS: The structure of RYMV was determined and refined to 2.8 A, resolution by X-ray crystallography. The capsid contains 180 copies of the, coat protein subunit arranged with T = 3 icosahedral symmetry. Each, subunit adopts a jelly-roll beta sandwich fold. The RYMV capsid structure, is similar to those of other sobemoviruses. When compared with these, viruses, however, the betaA arm of the RYMV C subunit, which is a, molecular switch that regulates quasi-equivalent subunit interactions, is, swapped with the 2-fold-related betaA arm to a similar, noncovalent, bonding environment. This exchange of identical structural elements across, a symmetry axis is categorized as 3D domain swapping and produces, long-range interactions throughout the icosahedral surface lattice., Biochemical analysis supports the notion that 3D domain swapping increases, the stability of RYMV. CONCLUSIONS: The quasi-equivalent interactions, between the RYMV proteins are regulated by the N-terminal ordered residues, of the betaA arm, which functions as a molecular switch. Comparative, analysis suggests that this molecular switch can also modulate the, stability of the viral capsids.

BACKGROUND: Rice yellow mottle virus (RYMV) is a major pathogen that dramatically reduces rice production in many African countries. RYMV belongs to the genus sobemovirus, one group of plant viruses with icosahedral capsids and single-stranded, positive-sense RNA genomes. RESULTS: The structure of RYMV was determined and refined to 2.8 A resolution by X-ray crystallography. The capsid contains 180 copies of the coat protein subunit arranged with T = 3 icosahedral symmetry. Each subunit adopts a jelly-roll beta sandwich fold. The RYMV capsid structure is similar to those of other sobemoviruses. When compared with these viruses, however, the betaA arm of the RYMV C subunit, which is a molecular switch that regulates quasi-equivalent subunit interactions, is swapped with the 2-fold-related betaA arm to a similar, noncovalent bonding environment. This exchange of identical structural elements across a symmetry axis is categorized as 3D domain swapping and produces long-range interactions throughout the icosahedral surface lattice. Biochemical analysis supports the notion that 3D domain swapping increases the stability of RYMV. CONCLUSIONS: The quasi-equivalent interactions between the RYMV proteins are regulated by the N-terminal ordered residues of the betaA arm, which functions as a molecular switch. Comparative analysis suggests that this molecular switch can also modulate the stability of the viral capsids.

==About this Structure==

1F2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rice_yellow_mottle_virus Rice yellow mottle virus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F2N OCA].

1F2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rice_yellow_mottle_virus Rice yellow mottle virus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2N OCA].

==Reference==

Line 13:

[[Category: Rice yellow mottle virus]]

[[Category: Single protein]]

[[Category: Beachy, R.N.]]

[[Category: Beachy, R N.]]

[[Category: Brugidou, C.]]

[[Category: Fauquet, C.M.]]

[[Category: Fauquet, C M.]]

[[Category: Johnson, J.E.]]

[[Category: Johnson, J E.]]

[[Category: Liljas, L.]]

[[Category: Lin, T.]]

Line 31:

[[Category: x-ray diffraction]]

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@@ Line 1: / Line 1: @@
-[[Image:1f2n.jpg|left|200px]]<br /><applet load="1f2n" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f2n.jpg|left|200px]]<br /><applet load="1f2n" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f2n, resolution 2.8&Aring;" />
 '''RICE YELLOW MOTTLE VIRUS'''<br />
 ==Overview==
-BACKGROUND: Rice yellow mottle virus (RYMV) is a major pathogen that, dramatically reduces rice production in many African countries. RYMV, belongs to the genus sobemovirus, one group of plant viruses with, icosahedral capsids and single-stranded, positive-sense RNA genomes., RESULTS: The structure of RYMV was determined and refined to 2.8 A, resolution by X-ray crystallography. The capsid contains 180 copies of the, coat protein subunit arranged with T = 3 icosahedral symmetry. Each, subunit adopts a jelly-roll beta sandwich fold. The RYMV capsid structure, is similar to those of other sobemoviruses. When compared with these, viruses, however, the betaA arm of the RYMV C subunit, which is a, molecular switch that regulates quasi-equivalent subunit interactions, is, swapped with the 2-fold-related betaA arm to a similar, noncovalent, bonding environment. This exchange of identical structural elements across, a symmetry axis is categorized as 3D domain swapping and produces, long-range interactions throughout the icosahedral surface lattice., Biochemical analysis supports the notion that 3D domain swapping increases, the stability of RYMV. CONCLUSIONS: The quasi-equivalent interactions, between the RYMV proteins are regulated by the N-terminal ordered residues, of the betaA arm, which functions as a molecular switch. Comparative, analysis suggests that this molecular switch can also modulate the, stability of the viral capsids.
+BACKGROUND: Rice yellow mottle virus (RYMV) is a major pathogen that dramatically reduces rice production in many African countries. RYMV belongs to the genus sobemovirus, one group of plant viruses with icosahedral capsids and single-stranded, positive-sense RNA genomes. RESULTS: The structure of RYMV was determined and refined to 2.8 A resolution by X-ray crystallography. The capsid contains 180 copies of the coat protein subunit arranged with T = 3 icosahedral symmetry. Each subunit adopts a jelly-roll beta sandwich fold. The RYMV capsid structure is similar to those of other sobemoviruses. When compared with these viruses, however, the betaA arm of the RYMV C subunit, which is a molecular switch that regulates quasi-equivalent subunit interactions, is swapped with the 2-fold-related betaA arm to a similar, noncovalent bonding environment. This exchange of identical structural elements across a symmetry axis is categorized as 3D domain swapping and produces long-range interactions throughout the icosahedral surface lattice. Biochemical analysis supports the notion that 3D domain swapping increases the stability of RYMV. CONCLUSIONS: The quasi-equivalent interactions between the RYMV proteins are regulated by the N-terminal ordered residues of the betaA arm, which functions as a molecular switch. Comparative analysis suggests that this molecular switch can also modulate the stability of the viral capsids.
 ==About this Structure==
-F2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rice_yellow_mottle_virus Rice yellow mottle virus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F2N OCA].
+F2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rice_yellow_mottle_virus Rice yellow mottle virus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2N OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rice yellow mottle virus]]
 [[Category: Single protein]]
-[[Category: Beachy, R.N.]]
+[[Category: Beachy, R N.]]
 [[Category: Brugidou, C.]]
-[[Category: Fauquet, C.M.]]
+[[Category: Fauquet, C M.]]
-[[Category: Johnson, J.E.]]
+[[Category: Johnson, J E.]]
 [[Category: Liljas, L.]]
 [[Category: Lin, T.]]
@@ Line 31: / Line 31: @@
 [[Category: x-ray diffraction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:11:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:11 2008''