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5chs

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Revision as of 12:28, 6 November 2017

N-terminal domain of the vesicular stomatitis virus L protein

Structural highlights

5chs is a 2 chain structure with sequence from Vsiv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[L_VSIVM] Displays RNA-directed RNA polymerase, mRNA guanylyl transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) synthetase activities. The viral mRNA guanylyl transferase displays a different biochemical reaction than the cellular enzyme. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). Functions either as transcriptase or as replicase. The transcriptase synthesizes subsequently five subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing the transcriptional signals (By similarity).

Publication Abstract from PubMed

Viruses have varied mechanisms to duplicate their genomes and produce viral specific mRNAs. Negative strand RNA viruses encode their own polymerases to perform each of these processes. For the nonsegmented negative-strand RNA viruses, the polymerase is comprised of the large polymerase subunit (L) and the phosphoprotein (P). L proteins from the Rhabdoviridae, Paramyxoviridae and Filoviridae share sequence and predicted secondary structure homology. Here, we present the structure of the N-terminal domain (conserved region I) of the L protein from a rhabdovirus, vesicular stomatitis virus, at 1.8A resolution. The strictly and strongly conserved residues in this domain cluster in a single area of the protein. Serial mutation of these residues shows that many of the amino acids are essential for viral transcription but not mRNA capping. Three-dimensional alignments show that this domain shares structural homology with polymerases from other viral families, included segmented negative-strand RNA and dsRNA viruses. IMPORTANCE: Negative strand RNA viruses include a diverse set of viral families that infect animals and plants causing serious illness and economic impact. This group of viruses share a common set of functionally conserved proteins that are essential to their replication cycle. Among this set of proteins is the viral polymerase, which performs a unique set of reactions to produce genomic- and subgenomic-length RNA transcripts. In this article, we study the polymerase of vesicular stomatitis virus, a member of the rhabdoviruses, which has served in the past as a model to study negative strand RNA virus replication. We have identified a site in the N-terminal domain of the polymerase that is essential to viral transcription and shares sequence homology with members of the paramyxoviruses and the filoviruses. Newly identified sites such as that described here could prove to be useful targets in the design of new therapeutics against negative strand RNA viruses.

Structure and function of the N-terminal domain of the vesicular stomatitis virus RNA polymerase.,Qiu S, Ogino M, Luo M, Ogino T, Green TJ J Virol. 2015 Oct 28. pii: JVI.02317-15. PMID:26512087^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Qiu S, Ogino M, Luo M, Ogino T, Green TJ. Structure and function of the N-terminal domain of the vesicular stomatitis virus RNA polymerase. J Virol. 2015 Oct 28. pii: JVI.02317-15. PMID:26512087 doi:http://dx.doi.org/10.1128/JVI.02317-15

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5chs"

@@ Line 1: / Line 1: @@
 ==N-terminal domain of the vesicular stomatitis virus L protein==
 <StructureSection load='5chs' size='340' side='right' caption='[[5chs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5chs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5chs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vsiv Vsiv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHS FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chs OCA], [http://pdbe.org/5chs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chs RCSB], [http://www.ebi.ac.uk/pdbsum/5chs PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chs OCA], [http://pdbe.org/5chs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chs RCSB], [http://www.ebi.ac.uk/pdbsum/5chs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5chs ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Vsiv]]
 [[Category: Green, T G]]
 [[Category: Luo, M]]

5chs

From Proteopedia

Revision as of 12:28, 6 November 2017

N-terminal domain of the vesicular stomatitis virus L protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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