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- SASDBQ3: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid ... -

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Basic information

Entry
Database: SASBDB / ID: SASDBQ3
SampleMiddle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
  • Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) (protein), MERS N-Protein, Middle East respiratory syndrome coronavirus
Function / homology
Function and homology information


viral nucleocapsid / ribonucleoprotein complex / RNA binding
Similarity search - Function
Nucleocapsid protein, coronavirus / Nucleocapsid protein, N-terminal / Nucleocapsid (N) protein, C-terminal domain, coronavirus / Nucleocapsid (N) protein, N-terminal domain, coronavirus / Coronavirus nucleocapsid / Coronavirus nucleocapsid (CoV N) protein N-terminal (NTD) domain profile. / Coronavirus nucleocapsid (CoV N) protein C-terminal (CTD) domain profile.
Similarity search - Domain/homology
Biological speciesMiddle East respiratory syndrome coronavirus
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2016
Title: Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Authors: Nicolas Papageorgiou / Julie Lichière / Amal Baklouti / François Ferron / Marion Sévajol / Bruno Canard / Bruno Coutard /
Abstract: The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N-terminal part is composed of an intrinsically disordered region (IDR) followed by a ...The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N-terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N-terminal domain (NTD). In this study, the structure determination of the N-terminal region of the MERS-CoV N protein via X-ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X-ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N-terminal region of the MERS-CoV as a monomer that displays structural features in common with other coronavirus NTDs.
Contact author
  • Nicolas Papageorgiou (CNRS, AFMB UMR 7257, 13288 Marseille, France)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #453
Type: dummy / Software: DAMMIF (r4556) / Radius of dummy atoms: 1.70 A / Chi-square value: 0.408 / P-value: 0.015000
Search similar-shape structures of this assembly by Omokage search (details)
Model #454
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 0.509
Search similar-shape structures of this assembly by Omokage search (details)
Model #455
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 0.509
Search similar-shape structures of this assembly by Omokage search (details)
Model #456
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 0.509
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
Specimen concentration: 0.21-3.06
BufferName: HEPES / Concentration: 10.00 mM / pH: 7.5 / Composition: 300 mM NaCl
Entity #303Name: MERS N-Protein / Type: protein
Description: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
Formula weight: 17.788 / Num. of mol.: 1 / Source: Middle East respiratory syndrome coronavirus / References: UniProt: T2B9R0
Sequence:
MASPAAPRAV SFADNNDITN TNLSRGRGRN PKPRAAPNNT VSWYTGLTQH GKVPLTFPPG QGVPLNANST PAQNAGYWRR QDRKINTGNG IKQLAPRWYF YYTGTGPEAA LPFRAVKDGI VWVHEDGATD APSTFGTRNP NNDSAIVTQF APGTKLPKNF HIEG

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
DetectorName: Pilatus 1M
Scan
Title: MERS N-Protein / Measurement date: Oct 5, 2015 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0364 4.9745
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 974 /
MinMax
Q0.159595 4.77073
P(R) point1 974
R0 8
Result
Type of curve: merged /
ExperimentalPorod
MW24.1 kDa-
Volume-27.5 nm3

P(R)Guinier
Forward scattering, I026.8 26.5
Radius of gyration, Rg2.04 nm1.95 nm

MinMax
D-8
Guinier point19 134

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