5NOH

HRSV M2-1 core domain

Summary for 5NOH

• Entry DOI: 10.2210/pdb5noh/pdb
• Descriptor: Transcription elongation factor M2-1 (2 entities in total)
• Functional Keywords: protein, transcription
• Biological source: Human respiratory syncytial virus
• Total number of polymer chains: 2
• Total formula weight: 23188.85

Authors

Josts, I.,Almeida Hernandez, Y.,Molina, I.G.,de Prat-Gay, G.,Tidow, H. (deposition date: 2017-04-12, release date: 2018-01-03, Last modification date: 2024-05-08)

Primary citation

Molina, I.G.,Josts, I.,Almeida Hernandez, Y.,Esperante, S.,Salgueiro, M.,Garcia Alai, M.M.,de Prat-Gay, G.,Tidow, H.
Structure and stability of the Human respiratory syncytial virus M2-1RNA-binding core domain reveals a compact and cooperative folding unit.
Acta Crystallogr F Struct Biol Commun, 74:23-30, 2018

PubMed Abstract: 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.

PubMed: 29372904
DOI: 10.1107/S2053230X17017381

Experimental method

X-RAY DIFFRACTION (1.8 Å)