Structural highlights
Function
[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Olal D, Daumke O. Structure of the Hantavirus Nucleoprotein Provides Insights into the Mechanism of RNA Encapsidation. Cell Rep. 2016 Mar 8;14(9):2092-9. doi: 10.1016/j.celrep.2016.02.005. Epub 2016, Feb 25. PMID:26923588 doi:http://dx.doi.org/10.1016/j.celrep.2016.02.005
