4qaz

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

spinqualitylabelsall models 4qaz, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qaz is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4qb0 Resources: FirstGlance, OCA, RCSB, PDBsum Function [NCAP_EBOZM] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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