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| - | ==The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein==
| + | #REDIRECT [[5e2x]] This PDB entry is obsolete and replaced by 5e2x |
| - | <StructureSection load='5cii' size='340' side='right' caption='[[5cii]], [[Resolution|resolution]] 2.10Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5cii]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CII FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qaz|4qaz]], [[4qb0|4qb0]]</td></tr>
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| - | <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=5cii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cii OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cii RCSB], [http://www.ebi.ac.uk/pdbsum/5cii PDBsum]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Ebolavirus (EBOV) causes severe hemorrhagic fever with a mortality rate of up to 90%. EBOV is a member of the order Mononegavirales and, like other viruses in this taxonomic group, contains a negative-sense single-stranded (ss) RNA. The EBOV ssRNA encodes seven distinct proteins. One of them, the nucleoprotein (NP), is the most abundant viral protein in the infected cell and within the viral nucleocapsid. Like other EBOV proteins, NP is multifunctional. It is tightly associated with the viral genome and is essential for viral transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. NP is unusual among the Mononegavirales in that it contains two distinct regions, or putative domains, the C-terminal of which shows no homology to any known proteins and is purported to be a hub for protein-protein interactions within the nucleocapsid. The atomic structure of NP remains unknown. Here, the boundaries of the N- and C-terminal domains of NP from Zaire EBOV are defined, it is shown that they can be expressed as highly stable recombinant proteins in Escherichia coli, and the atomic structure of the C-terminal domain (residues 641-739) derived from analysis of two distinct crystal forms at 1.98 and 1.75 A resolution is described. The structure reveals a novel tertiary fold that is distantly reminiscent of the beta-grasp architecture.
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| - | The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein.,Dziubanska PJ, Derewenda U, Ellena JF, Engel DA, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2420-9. doi:, 10.1107/S1399004714014710. Epub 2014 Aug 29. PMID:25195755<ref>PMID:25195755</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Baker, L E]]
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| - | [[Category: Derewenda, U]]
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| - | [[Category: Derewenda, Z S]]
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| - | [[Category: Handing, K B]]
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| - | [[Category: Utepbergenov, D]]
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| - | [[Category: Viral protein]]
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