Structural highlights
Function
[VP4A_LNYV3] Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
Publication Abstract from PubMed
Lettuce necrotic yellows virus (LNYV) is a prototype of the plant-adapted cytorhabdoviruses. Through a meta-prediction of disorder, we localized a folded C-terminal domain in the amino acid sequence of its phosphoprotein. This domain consists of an autonomous folding unit that is monomeric in solution. Its structure, solved by X-ray crystallography, reveals a lollipop-shaped structure comprising five helices. The structure is different from that of the corresponding domains of other Rhabdoviridae, Filoviridae, and Paramyxovirinae; only the overall topology of the polypeptide chain seems to be conserved, suggesting that this domain evolved under weak selective pressure and varied in size by the acquisition or loss of functional modules.
Structure of the C-terminal domain of lettuce necrotic yellows virus phosphoprotein.,Martinez N, Ribeiro EA Jr, Leyrat C, Tarbouriech N, Ruigrok RW, Jamin M J Virol. 2013 Sep;87(17):9569-78. doi: 10.1128/JVI.00999-13. Epub 2013 Jun 19. PMID:23785215[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martinez N, Ribeiro EA Jr, Leyrat C, Tarbouriech N, Ruigrok RW, Jamin M. Structure of the C-terminal domain of lettuce necrotic yellows virus phosphoprotein. J Virol. 2013 Sep;87(17):9569-78. doi: 10.1128/JVI.00999-13. Epub 2013 Jun 19. PMID:23785215 doi:http://dx.doi.org/10.1128/JVI.00999-13
