1f2n
From Proteopedia
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| - | [[Image:1f2n.jpg|left|200px]] | + | [[Image:1f2n.jpg|left|200px]] |
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| - | '''RICE YELLOW MOTTLE VIRUS''' | + | {{Structure |
| + | |PDB= 1f2n |SIZE=350|CAPTION= <scene name='initialview01'>1f2n</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RICE YELLOW MOTTLE VIRUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F2N is a [ | + | 1F2N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rice_yellow_mottle_virus Rice yellow mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2N OCA]. |
==Reference== | ==Reference== | ||
| - | 3D domain swapping modulates the stability of members of an icosahedral virus group., Qu C, Liljas L, Opalka N, Brugidou C, Yeager M, Beachy RN, Fauquet CM, Johnson JE, Lin T, Structure. 2000 Oct 15;8(10):1095-103. PMID:[http:// | + | 3D domain swapping modulates the stability of members of an icosahedral virus group., Qu C, Liljas L, Opalka N, Brugidou C, Yeager M, Beachy RN, Fauquet CM, Johnson JE, Lin T, Structure. 2000 Oct 15;8(10):1095-103. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080631 11080631] |
[[Category: Rice yellow mottle virus]] | [[Category: Rice yellow mottle virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:31 2008'' |
Revision as of 09:03, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
RICE YELLOW MOTTLE VIRUS
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.
About this Structure
1F2N is a Single protein structure of sequence from Rice yellow mottle virus. Full crystallographic information is available from OCA.
Reference
3D domain swapping modulates the stability of members of an icosahedral virus group., Qu C, Liljas L, Opalka N, Brugidou C, Yeager M, Beachy RN, Fauquet CM, Johnson JE, Lin T, Structure. 2000 Oct 15;8(10):1095-103. PMID:11080631
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