View source for 3jsb


==Crystal structure of the N-terminal domain of the Lymphocytic Choriomeningitis Virus L protein==
<StructureSection load='3jsb' size='340' side='right' caption='[[3jsb]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3jsb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lcmv Lcmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JSB FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11624 LCMV])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=3jsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jsb OCA], [http://pdbe.org/3jsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jsb RCSB], [http://www.ebi.ac.uk/pdbsum/3jsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jsb ProSAT]</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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/3jsb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3jsb ConSurf].
<div style="clear:both"></div>
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== 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<ref>PMID:20862324</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3jsb" style="background-color:#fffaf0;"></div>

==See Also==
*[[RNA polymerase|RNA polymerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lcmv]]
[[Category: RNA-directed RNA polymerase]]
[[Category: Bricogne, G]]
[[Category: Canard, B]]
[[Category: Coutard, B]]
[[Category: Ferron, F P]]
[[Category: Jamal, S]]
[[Category: Structural genomic]]
[[Category: Morin, B]]
[[Category: Vonrhein, C]]
[[Category: Msgp]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotidyltransferase]]
[[Category: Rna binding protein]]
[[Category: Rna replication]]
[[Category: Rna-directed rna polymerase]]
[[Category: Transferase]]
[[Category: Viral protein]]
[[Category: Virion]]
[[Category: Vizier]]