6HAT

Globular domain of herpesvirus saimiri ORF57

6HAT の概要

• エントリーDOI: 10.2210/pdb6hat/pdb
• 分子名称: mRNA export factor ICP27 homolog, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: homodimer, icp27, ihd, rna, rna binding protein
• 由来する生物種: Saimiriine herpesvirus 2 (strain 11) (SaHV-2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62383.66

構造登録者

Tunnicliffe, R.B.,Levy, C.,Ruiz Nivia, H.D.,Sandri-Goldin, R.M.,Golovanov, A.P. (登録日: 2018-08-08, 公開日: 2018-11-21, 最終更新日: 2024-10-16)

主引用文献

Tunnicliffe, R.B.,Levy, C.,Ruiz Nivia, H.D.,Sandri-Goldin, R.M.,Golovanov, A.P.
Structural identification of conserved RNA binding sites in herpesvirus ORF57 homologs: implications for PAN RNA recognition.
Nucleic Acids Res., 47:1987-2001, 2019

PubMed Abstract: Kaposi's sarcoma-associated herpesvirus (KSHV) transcribes a long noncoding polyadenylated nuclear (PAN) RNA, which promotes the latent to lytic transition by repressing host genes involved in antiviral responses as well as viral proteins that support the latent state. KSHV also expresses several early proteins including ORF57 (Mta), a member of the conserved multifunctional ICP27 protein family, which is essential for productive replication. ORF57/Mta interacts with PAN RNA via a region termed the Mta responsive element (MRE), stabilizing the transcript and supporting nuclear accumulation. Here, using a close homolog of KSHV ORF57 from herpesvirus saimiri (HVS), we determined the crystal structure of the globular domain in complex with a PAN RNA MRE, revealing a uracil specific binding site that is also conserved in KSHV. Using solution NMR, RNA binding was also mapped within the disordered N-terminal domain of KSHV ORF57, and showed specificity for an RNA fragment containing a GAAGRG motif previously known to bind a homologous region in HVS ORF57. Together these data located novel differential RNA recognition sites within neighboring domains of herpesvirus ORF57 homologs, and revealed high-resolution details of their interactions with PAN RNA, thus providing insight into interactions crucial to viral function.

PubMed: 30462297
DOI: 10.1093/nar/gky1181

実験手法

X-RAY DIFFRACTION (1.856 Å)