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TitleStructure and stability of the Human respiratory syncytial virus M RNA-binding core domain reveals a compact and cooperative folding unit.
Journal, issue, pagesActa Crystallogr F Struct Biol Commun, Vol. 74, Issue Pt 1, Page 23-30, Year 2018
Publish dateJan 1, 2018
AuthorsIvana G Molina / Inokentijs Josts / Yasser Almeida Hernandez / Sebastian Esperante / Mariano Salgueiro / Maria M Garcia Alai / Gonzalo de Prat-Gay / Henning Tidow /
PubMed AbstractHuman syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, ...Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M. The puzzling mechanism of action of M, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M tetramer, with additional electron density for the C-terminal tail that was not observed in the previous models. Moreover, its folding stability was determined through chemical denaturation, which shows that the secondary and tertiary structure unfold concomitantly, which is indicative of a two-state equilibrium. These results constitute a further step in the understanding of this unique RNA-binding domain, for which there is no sequence or structural counterpart outside this virus family, in addition to its implications in transcription regulation and its likeliness as an antiviral target.
External linksActa Crystallogr F Struct Biol Commun / PubMed:29372904 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.8 - 2.00008687185 Å
Structure data

SASDDE3:
Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain
Method: SAXS/SANS

PDB-5nkx:
HRSV M2-1 core domain, P3221 crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.00008687185 Å

PDB-5noh:
HRSV M2-1 core domain
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Human orthopneumovirus
  • human respiratory syncytial virus
KeywordsVIRAL PROTEIN / TRANSCRIPTION / protein

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