5dsd: Difference between revisions

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New page: ==The crystal structure of the C-terminal domain of Ebola (Bundibugyo) nucleoprotein== <StructureSection load='5dsd' size='340' side='right' caption='5dsd, resolution 2....
 
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Revision as of 17:29, 30 September 2015

The crystal structure of the C-terminal domain of Ebola (Bundibugyo) nucleoproteinThe crystal structure of the C-terminal domain of Ebola (Bundibugyo) nucleoprotein

Structural highlights

5dsd is a 1 chain structure. This structure supersedes the now removed PDB entry 5cij. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Publication Abstract from PubMed

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.

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[1]

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

References

  1. Dziubanska PJ, Derewenda U, Ellena JF, Engel DA, Derewenda ZS. The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein. Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2420-9. doi:, 10.1107/S1399004714014710. Epub 2014 Aug 29. PMID:25195755 doi:http://dx.doi.org/10.1107/S1399004714014710

5dsd, resolution 2.31Å

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OCA