3t5q: Difference between revisions
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[[ | ==3A structure of Lassa virus nucleoprotein in complex with ssRNA== | ||
<StructureSection load='3t5q' size='340' side='right' caption='[[3t5q]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t5q]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mopeia_lassa_reassortant_29 Mopeia lassa reassortant 29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T5Q FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t5n|3t5n]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300180 Mopeia Lassa reassortant 29])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t5q RCSB], [http://www.ebi.ac.uk/pdbsum/3t5q PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Arenaviruses cause disease in industrialized and developing nations alike. Among them, the hemorrhagic fever virus Lassa is responsible for ~300,000-500,000 infections/y in Western Africa. The arenavirus nucleoprotein (NP) forms the protein scaffold of the genomic ribonucleoprotein complexes and is critical for transcription and replication of the viral genome. Here, we present crystal structures of the RNA-binding domain of Lassa virus NP in complex with ssRNA. This structure shows, in contrast to the predicted model, that RNA binds in a deep, basic crevice located entirely within the N-terminal domain. Furthermore, the NP-ssRNA structures presented here, combined with hydrogen-deuterium exchange/MS and functional studies, suggest a gating mechanism by which NP opens to accept RNA. Directed mutagenesis and functional studies provide a unique look into how the arenavirus NPs bind to and protect the viral genome and also suggest the likely assembly by which viral ribonucleoprotein complexes are organized. | |||
Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding.,Hastie KM, Liu T, Li S, King LB, Ngo N, Zandonatti MA, Woods VL Jr, de la Torre JC, Saphire EO Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19365-70. Epub 2011 Nov 14. PMID:22084115<ref>PMID:22084115</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Nucleoprotein|Nucleoprotein]] | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Mopeia lassa reassortant 29]] | [[Category: Mopeia lassa reassortant 29]] | ||
Revision as of 09:09, 5 June 2014
3A structure of Lassa virus nucleoprotein in complex with ssRNA3A structure of Lassa virus nucleoprotein in complex with ssRNA
Structural highlights
Publication Abstract from PubMedArenaviruses cause disease in industrialized and developing nations alike. Among them, the hemorrhagic fever virus Lassa is responsible for ~300,000-500,000 infections/y in Western Africa. The arenavirus nucleoprotein (NP) forms the protein scaffold of the genomic ribonucleoprotein complexes and is critical for transcription and replication of the viral genome. Here, we present crystal structures of the RNA-binding domain of Lassa virus NP in complex with ssRNA. This structure shows, in contrast to the predicted model, that RNA binds in a deep, basic crevice located entirely within the N-terminal domain. Furthermore, the NP-ssRNA structures presented here, combined with hydrogen-deuterium exchange/MS and functional studies, suggest a gating mechanism by which NP opens to accept RNA. Directed mutagenesis and functional studies provide a unique look into how the arenavirus NPs bind to and protect the viral genome and also suggest the likely assembly by which viral ribonucleoprotein complexes are organized. Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding.,Hastie KM, Liu T, Li S, King LB, Ngo N, Zandonatti MA, Woods VL Jr, de la Torre JC, Saphire EO Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19365-70. Epub 2011 Nov 14. PMID:22084115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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