5fsg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the hantavirus nucleoprotein provides insights into the mechanism of RNA encapsidation and a template for drug design== | |
| + | <StructureSection load='5fsg' size='340' side='right'caption='[[5fsg]], [[Resolution|resolution]] 3.21Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hantaan_virus_76-118 Hantaan virus 76-118]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FSG FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.209Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fsg OCA], [https://pdbe.org/5fsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fsg RCSB], [https://www.ebi.ac.uk/pdbsum/5fsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fsg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/NCAP_HANTV NCAP_HANTV] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hantaviruses are etiological agents of life-threatening hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome. The nucleoprotein (N) of hantavirus is essential for viral transcription and replication, thus representing an attractive target for therapeutic intervention. We have determined the crystal structure of hantavirus N to 3.2 A resolution. The structure reveals a two-lobed, mostly alpha-helical structure that is distantly related to that of orthobunyavirus Ns. A basic RNA binding pocket is located at the intersection between the two lobes. We provide evidence that oligomerization is mediated by amino- and C-terminal arms that bind to the adjacent monomers. Based on these findings, we suggest a model for the oligomeric ribonucleoprotein (RNP) complex. Our structure provides mechanistic insights into RNA encapsidation in the genus Hantavirus and constitutes a template for drug discovery efforts aimed at combating hantavirus infections. | ||
| - | + | Structure of the Hantavirus Nucleoprotein Provides Insights into the Mechanism of RNA Encapsidation.,Olal D, Daumke O Cell Rep. 2016 Mar 8;14(9):2092-9. doi: 10.1016/j.celrep.2016.02.005. Epub 2016, Feb 25. PMID:26923588<ref>PMID:26923588</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5fsg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Daumke | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hantaan virus 76-118]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Daumke O]] | ||
| + | [[Category: Olal D]] | ||
Current revision
Structure of the hantavirus nucleoprotein provides insights into the mechanism of RNA encapsidation and a template for drug design
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