[English] 日本語
Yorodumi
- PDB-5c8u: Crystal structure of the SARS coronavirus nsp14-nsp10 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5c8u
TitleCrystal structure of the SARS coronavirus nsp14-nsp10 complex
Components
  • Guanine-N7 methyltransferase
  • Non-structural protein 10
KeywordsTRANSFERASE / nsp14 / nsp10 / exoribonuclease / methyl transferase
Function / homology
Function and homology information


Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / Transcription of SARS-CoV-1 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-1 genome / K48-linked deubiquitinase activity / host cell endoplasmic reticulum / K63-linked deubiquitinase activity / SARS-CoV-1 modulates host translation machinery / viral transcription ...Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / Transcription of SARS-CoV-1 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-1 genome / K48-linked deubiquitinase activity / host cell endoplasmic reticulum / K63-linked deubiquitinase activity / SARS-CoV-1 modulates host translation machinery / viral transcription / Transferases; Transferring one-carbon groups; Methyltransferases / SARS-CoV-1 activates/modulates innate immune responses / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / double membrane vesicle viral factory outer membrane / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / SARS coronavirus main proteinase / host cell endosome / 3'-5'-RNA exonuclease activity / : / host cell endoplasmic reticulum-Golgi intermediate compartment / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / omega peptidase activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / mRNA (nucleoside-2'-O-)-methyltransferase activity / endonuclease activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ATP hydrolysis activity / proteolysis / zinc ion binding / ATP binding / membrane / identical protein binding
Similarity search - Function
Non-structural protein 3, SUD-N macrodomain, SARS-CoV / RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : ...Non-structural protein 3, SUD-N macrodomain, SARS-CoV / RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / NSP12 RNA-dependent RNA polymerase, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidovirus 2-O-methyltransferase / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nonstructural protein 13, 1B domain, coronavirus / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerization / Nonstructural protein 15, middle domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein NSP3, N-terminal, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus SUD-C domain / Betacoronavirus replicase NSP3, N-terminal / NSP1 globular domain superfamily, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Coronavirus 3Ecto domain profile. / : / Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile. / NSP1, C-terminal domain, betacoronavirus / Betacoronavirus Nsp3c-M domain profile. / NSP1, globular domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Betacoronavirus replicase NSP1 / Betacoronavirus single-stranded poly(A) binding domain / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Betacoronavirus Nsp3c-C domain profile. / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Non-structural protein NSP3A domain-like superfamily / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / : / Coronavirus (CoV) Nsp2 middle domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / NSP1, globular domain, alpha/betacoronavirus / : / Coronavirus (CoV) Nsp3 Y domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Coronavirus Nsp4 C-terminal (Nsp4C) domain profile.
Similarity search - Domain/homology
Replicase polyprotein 1ab
Similarity search - Component
Biological speciesHuman SARS coronavirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.401 Å
AuthorsMa, Y.Y. / Wu, L.J. / Zhang, R.G. / Rao, Z.H.
Funding support China, 4items
OrganizationGrant numberCountry
Ministry of Science and Technology of China Project 9732014CB542800 China
Ministry of Science and Technology of China Project 9732014CBA02003 China
National Natural Science Foundation of China81330036 China
Strategic Priority Research Program of the Chinese Academy of SciencesXDB08020200 China
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2015
Title: Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex
Authors: Ma, Y.Y. / Wu, L.J. / Shaw, N. / Gao, Y. / Wang, J. / Sun, Y.N. / Lou, Z.Y. / Yan, L.M. / Zhang, R.G. / Rao, Z.H.
History
DepositionJun 26, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jul 15, 2015Provider: repository / Type: Initial release
Revision 1.1Aug 12, 2015Group: Database references
Revision 1.2Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Non-structural protein 10
B: Guanine-N7 methyltransferase
C: Non-structural protein 10
D: Guanine-N7 methyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,43716
Polymers150,7344
Non-polymers70312
Water0
1
A: Non-structural protein 10
B: Guanine-N7 methyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,7188
Polymers75,3672
Non-polymers3516
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4540 Å2
ΔGint-38 kcal/mol
Surface area29880 Å2
MethodPISA
2
C: Non-structural protein 10
D: Guanine-N7 methyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,7188
Polymers75,3672
Non-polymers3516
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4360 Å2
ΔGint-40 kcal/mol
Surface area29940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)189.928, 194.979, 179.844
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221

-
Components

#1: Protein Non-structural protein 10 / nsp10


Mass: 15268.438 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human SARS coronavirus / Production host: Escherichia coli (E. coli) / References: UniProt: P0C6X7
#2: Protein Guanine-N7 methyltransferase / nsp14


Mass: 60098.605 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human SARS coronavirus / Production host: Escherichia coli (E. coli)
References: UniProt: P0C6X7, Transferases; Transferring one-carbon groups; Methyltransferases, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 5.58 Å3/Da / Density % sol: 77.97 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop
Details: 15% (v/v) tacsimate pH 7.0, 0.1 M HEPES pH 7.0, 2% (w/v) polyethylene glycol 3350

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.984 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Sep 18, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.984 Å / Relative weight: 1
ReflectionResolution: 3.4→50 Å / Num. obs: 46052 / % possible obs: 100 % / Redundancy: 7.5 % / Biso Wilson estimate: 109.91 Å2 / Rmerge(I) obs: 0.086 / Rpim(I) all: 0.033 / Rrim(I) all: 0.092 / Χ2: 1.164 / Net I/av σ(I): 26.83 / Net I/σ(I): 9.6 / Num. measured all: 346535
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Num. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible allRmerge(I) obs
3.4-3.467.422360.8310.3590.9861.017100
3.46-3.527.522780.8960.2920.8041.0441000.749
3.52-3.597.623100.9180.250.6911.0221000.644
3.59-3.667.622580.9390.2140.5931.0281000.553
3.66-3.747.622670.960.1780.4921.0541000.459
3.74-3.837.622860.9760.1380.3831.0381000.357
3.83-3.927.622710.9830.1180.3271.0811000.305
3.92-4.037.623050.9890.0890.2471.0311000.231
4.03-4.157.622820.9930.0670.1871.0271000.174
4.15-4.287.622990.9960.0550.1521.0441000.141
4.28-4.447.622830.9970.0430.121.1031000.111
4.44-4.617.622960.9980.0370.1031.2541000.096
4.61-4.827.622880.9970.0370.1021.4451000.095
4.82-5.087.623080.9970.0310.0861.3991000.08
5.08-5.47.623150.9980.0280.0771.2691000.071
5.4-5.817.523090.9980.0250.0691.1941000.064
5.81-6.47.523210.9990.020.0561.1841000.052
6.4-7.327.523370.9990.0160.0441.231000.041
7.32-9.217.4235710.0120.0331.2911000.031
9.21-506.824460.9990.0110.031.54699.30.027

-
Processing

Software
NameVersionClassification
HKL-3000data scaling
PHENIX1.7.1_743refinement
PDB_EXTRACT3.15data extraction
HKL-3000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.401→45.35 Å / FOM work R set: 0.7587 / SU ML: 0.83 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2663 2326 5.06 %Random selection
Rwork0.2179 43673 --
obs0.2203 45999 99.85 %-
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 99.973 Å2 / ksol: 0.314 e/Å3
Displacement parametersBiso max: 335.16 Å2 / Biso mean: 151.57 Å2 / Biso min: 56.4 Å2
Baniso -1Baniso -2Baniso -3
1--27.3705 Å20 Å2-0 Å2
2--60.6365 Å20 Å2
3----33.2661 Å2
Refinement stepCycle: final / Resolution: 3.401→45.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10160 0 12 0 10172
Biso mean--167.79 --
Num. residues----1294
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02410542
X-RAY DIFFRACTIONf_angle_d1.34314246
X-RAY DIFFRACTIONf_chiral_restr0.091540
X-RAY DIFFRACTIONf_plane_restr0.0061828
X-RAY DIFFRACTIONf_dihedral_angle_d19.193716
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 17

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.4012-3.47060.39931240.33512525264999
3.4706-3.54610.40981420.314825192661100
3.5461-3.62850.33821410.293825272668100
3.6285-3.71920.34661270.275325482675100
3.7192-3.81970.37751440.257925472691100
3.8197-3.93210.29171400.241725342674100
3.9321-4.05890.26391480.233425342682100
4.0589-4.20390.25271310.209325602691100
4.2039-4.37210.24761450.197325652710100
4.3721-4.57090.21541330.185925642697100
4.5709-4.81160.23741440.168325562700100
4.8116-5.11270.25351280.185725832711100
5.1127-5.50680.26111400.210225682708100
5.5068-6.05990.28371210.229526002721100
6.0599-6.9340.2661260.214326102736100
6.934-8.7260.25731430.191626332776100
8.726-45.3540.23231490.2162700284999
Refinement TLS params.Method: refined / Origin x: -17.9809 Å / Origin y: -62.7553 Å / Origin z: -10.124 Å
111213212223313233
T0.7938 Å2-0.0392 Å2-0.2417 Å2-0.7624 Å2-0.2138 Å2--0.7957 Å2
L0.2213 °2-0.0841 °20.2239 °2-0.0458 °2-0.5009 °2--0.1651 °2
S-0.265 Å °0.1452 Å °0.0153 Å °-0.1102 Å °0.1096 Å °0.0089 Å °-0.2555 Å °-0.0662 Å °-0.0029 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA-1 - 202
2X-RAY DIFFRACTION1allB1 - 604
3X-RAY DIFFRACTION1allC-1 - 202
4X-RAY DIFFRACTION1allD1 - 604

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more