3jsb

From Proteopedia

(Difference between revisions)

Revision as of 14:15, 24 December 2014

Crystal structure of the N-terminal domain of the Lymphocytic Choriomeningitis Virus L protein

Structural highlights

3jsb is a 2 chain structure with sequence from Lymphocytic choriomeningitis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	L (Lymphocytic choriomeningitis virus)
Activity:	RNA-directed RNA polymerase, with EC number 2.7.7.48
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[L_LYCVA] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Arenaviridae synthesize viral mRNAs using short capped primers presumably acquired from cellular transcripts by a 'cap-snatching' mechanism. Here, we report the crystal structure and functional characterization of the N-terminal 196 residues (NL1) of the L protein from the prototypic arenavirus: lymphocytic choriomeningitis virus. The NL1 domain is able to bind and cleave RNA. The 2.13 A resolution crystal structure of NL1 reveals a type II endonuclease alpha/beta architecture similar to the N-terminal end of the influenza virus PA protein. Superimposition of both structures, mutagenesis and reverse genetics studies reveal a unique spatial arrangement of key active site residues related to the PD...(D/E)XK type II endonuclease signature sequence. We show that this endonuclease domain is conserved and active across the virus families Arenaviridae, Bunyaviridae and Orthomyxoviridae and propose that the arenavirus NL1 domain is the Arenaviridae cap-snatching endonuclease.

The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription.,Morin B, Coutard B, Lelke M, Ferron F, Kerber R, Jamal S, Frangeul A, Baronti C, Charrel R, de Lamballerie X, Vonrhein C, Lescar J, Bricogne G, Gunther S, Canard B PLoS Pathog. 2010 Sep 16;6(9). pii: e1001038. PMID:20862324^[2]

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

References

↑ Meyer BJ, Southern PJ. Concurrent sequence analysis of 5' and 3' RNA termini by intramolecular circularization reveals 5' nontemplated bases and 3' terminal heterogeneity for lymphocytic choriomeningitis virus mRNAs. J Virol. 1993 May;67(5):2621-7. PMID:7682625
↑ Morin B, Coutard B, Lelke M, Ferron F, Kerber R, Jamal S, Frangeul A, Baronti C, Charrel R, de Lamballerie X, Vonrhein C, Lescar J, Bricogne G, Gunther S, Canard B. The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription. PLoS Pathog. 2010 Sep 16;6(9). pii: e1001038. PMID:20862324 doi:10.1371/journal.ppat.1001038

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3jsb"

@@ Line 7: / Line 7: @@
 <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=3jsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jsb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jsb RCSB], [http://www.ebi.ac.uk/pdbsum/3jsb PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/L_LYCVA L_LYCVA]] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.<ref>PMID:7682625</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3jsb

From Proteopedia

Revision as of 14:15, 24 December 2014

Crystal structure of the N-terminal domain of the Lymphocytic Choriomeningitis Virus L protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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