2gu0
From Proteopedia
(New page: 200px<br /><applet load="2gu0" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gu0, resolution 2.800Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
| - | Viral inclusion bodies, or viroplasms, that form in rotavirus-infected | + | Viral inclusion bodies, or viroplasms, that form in rotavirus-infected cells direct replication and packaging of the segmented double-stranded RNA (dsRNA) genome. NSP2, one of two rotavirus proteins needed for viroplasm assembly, possesses NTPase, RNA-binding, and helix-unwinding activities. NSP2 of the rotavirus group causing endemic infantile diarrhea (group A) was shown to self-assemble into large doughnut-shaped octamers with circumferential grooves and deep clefts containing nucleotide-binding histidine triad (HIT)-like motifs. Here, we demonstrate that NSP2 of group C rotavirus, a group that fails to reassort with group A viruses, retains the unique architecture of the group A octamer but differs in surface charge distribution. By using an NSP2-dependent complementation system, we show that the HIT-dependent NTPase activity of NSP2 is necessary for dsRNA synthesis, but not for viroplasm formation. The complementation system also showed that despite the retention of the octamer structure and the HIT-like fold, group C NSP2 failed to rescue replication and viroplasm formation in NSP2-deficient cells infected with group A rotavirus. The distinct differences in the surface charges on the Bristol and SA11 NSP2 octamers suggest that charge complementarity of the viroplasm-forming proteins guides the specificity of viroplasm formation and, possibly, reassortment restriction between rotavirus groups. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jiang, X.]] | [[Category: Jiang, X.]] | ||
| - | [[Category: Prasad, B | + | [[Category: Prasad, B V.V.]] |
[[Category: bristol]] | [[Category: bristol]] | ||
[[Category: hit motif]] | [[Category: hit motif]] | ||
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[[Category: rotavirus]] | [[Category: rotavirus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:35:20 2008'' |
Revision as of 15:35, 21 February 2008
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Crystal Structure of Human Rotavirus NSP2 (Group C / Bristol Strain)
Overview
Viral inclusion bodies, or viroplasms, that form in rotavirus-infected cells direct replication and packaging of the segmented double-stranded RNA (dsRNA) genome. NSP2, one of two rotavirus proteins needed for viroplasm assembly, possesses NTPase, RNA-binding, and helix-unwinding activities. NSP2 of the rotavirus group causing endemic infantile diarrhea (group A) was shown to self-assemble into large doughnut-shaped octamers with circumferential grooves and deep clefts containing nucleotide-binding histidine triad (HIT)-like motifs. Here, we demonstrate that NSP2 of group C rotavirus, a group that fails to reassort with group A viruses, retains the unique architecture of the group A octamer but differs in surface charge distribution. By using an NSP2-dependent complementation system, we show that the HIT-dependent NTPase activity of NSP2 is necessary for dsRNA synthesis, but not for viroplasm formation. The complementation system also showed that despite the retention of the octamer structure and the HIT-like fold, group C NSP2 failed to rescue replication and viroplasm formation in NSP2-deficient cells infected with group A rotavirus. The distinct differences in the surface charges on the Bristol and SA11 NSP2 octamers suggest that charge complementarity of the viroplasm-forming proteins guides the specificity of viroplasm formation and, possibly, reassortment restriction between rotavirus groups.
About this Structure
2GU0 is a Single protein structure of sequence from Human rotavirus (group c/strain bristol). Full crystallographic information is available from OCA.
Reference
Structure-function analysis of rotavirus NSP2 octamer by using a novel complementation system., Taraporewala ZF, Jiang X, Vasquez-Del Carpio R, Jayaram H, Prasad BV, Patton JT, J Virol. 2006 Aug;80(16):7984-94. PMID:16873255
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