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

Basic information

• Entry: Database: SASBDB / ID: SASDDE3

Sample

Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain

• Human respiratory syncytial virus M2-1 (protein), HRSV M2-1, Human orthopneumovirus

Function / homology

Function:

: / regulation of viral transcription / viral transcription / translation elongation factor activity / virion component / transcription antitermination / host cell cytoplasm / structural constituent of virion / host cell nucleus / RNA binding / metal ion binding

Domain/homology:

Pneumovirus matrix 2-1 / Pneumovirus matrix protein 2 (M2) / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile.

Component:

Protein M2-1

• Biological species: Human orthopneumovirus
• Citation: Journal: Acta Crystallogr F Struct Biol Commun / Year: 2018; Title: Structure and stability of the Human respiratory syncytial virus M RNA-binding core domain reveals a compact and cooperative folding unit.; Authors: Ivana G Molina / Inokentijs Josts / Yasser Almeida Hernandez / Sebastian Esperante / Mariano Salgueiro / Maria M Garcia Alai / Gonzalo de Prat-Gay / Henning Tidow / ; 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.

Contact author

• Yasser Almeida (University of Hamburg, Hamburg, Germany)

Models

• Model #1777: ; Type: dummy / Radius of dummy atoms: 1.75 A / Chi-square value: 1.232 / P-value: 0.039236; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain; Specimen concentration: 4.50-9.00
• Buffer: Name: 20 mM Tris–HCl, 300 mM NaCl, / pH: 7

Entity #963

Name: HRSV M2-1 / Type: protein / Description: Human respiratory syncytial virus M2-1 / Formula weight: 13.658 / Num. of mol.: 1 / Source: Human orthopneumovirus / References: UniProt: Q4KRW3
Sequence:

ALGVVGVLES YIGSINNITK QSACVAMSKL LTELNSDDIK KLRDNEELNS PKIRVYNTVI SYIESNRKNN KQTIHLLKRL PADVLKKTIK NTLDIHKSIT INNPKELTVS DTNDHAKNND TT

Experimental information

• Beam: Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3 mm
• Detector: Name: Pilatus 2M

Scan

Title: Human respiratory syncytial virus (HRSV) M 2–1 RNA-binding core domain
Measurement date: Dec 13, 2016 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.045 sec. / Number of frames: 20 / Unit: 1/nm /

	Min	Max
Q	0.0195	5.0075

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 1325 /

	Min	Max
Q	0.225008	3.85364
P(R) point	1	1325
R	0	7.9

Result

Type of curve: single_conc /

	Experimental	Porod
MW	15 kDa	15 kDa
Volume	-	2.64 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	3865	5.1	3828.08	3.24
Radius of gyration, Rg	2.14 nm	0.005	2.03 nm	-

	Min	Max
D	-	7.9
Guinier point	63	228