2fqm
From Proteopedia
(New page: 200px<br /><applet load="2fqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fqm, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:2fqm.gif|left|200px]]<br /><applet load="2fqm" size=" | + | [[Image:2fqm.gif|left|200px]]<br /><applet load="2fqm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fqm, resolution 2.3Å" /> | caption="2fqm, resolution 2.3Å" /> | ||
'''Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus'''<br /> | '''Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the replication cycle of nonsegmented negative-strand RNA viruses, the | + | In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-angstroms-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a beta hairpin, an alpha helix, and another beta hairpin. The alpha helix provides the stabilizing force for forming a homodimer, while the two beta hairpins add additional stabilization by forming a four-stranded beta sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template. |
==About this Structure== | ==About this Structure== | ||
| - | 2FQM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vesicular_stomatitis_indiana_virus Vesicular stomatitis indiana virus]. Full crystallographic information is available from [http:// | + | 2FQM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vesicular_stomatitis_indiana_virus Vesicular stomatitis indiana virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Vesicular stomatitis indiana virus]] | [[Category: Vesicular stomatitis indiana virus]] | ||
[[Category: Ding, H.]] | [[Category: Ding, H.]] | ||
| - | [[Category: Green, T | + | [[Category: Green, T J.]] |
[[Category: Lu, S.]] | [[Category: Lu, S.]] | ||
[[Category: Luo, M.]] | [[Category: Luo, M.]] | ||
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[[Category: replication]] | [[Category: replication]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:15 2008'' |
Revision as of 15:24, 21 February 2008
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Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
Overview
In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-angstroms-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a beta hairpin, an alpha helix, and another beta hairpin. The alpha helix provides the stabilizing force for forming a homodimer, while the two beta hairpins add additional stabilization by forming a four-stranded beta sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template.
About this Structure
2FQM is a Single protein structure of sequence from Vesicular stomatitis indiana virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus., Ding H, Green TJ, Lu S, Luo M, J Virol. 2006 Mar;80(6):2808-14. PMID:16501089
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