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- PDB-4owr: Vesiculoviral matrix (M) protein occupies nucleic acid binding si... -

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Basic information

Entry
Database: PDB / ID: 4owr
TitleVesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair Rae1-Nup98
Components
  • Matrix protein
  • Nuclear pore complex protein Nup98-Nup96
  • mRNA export factor
KeywordsTRANSPORT PROTEIN / mRNA export / virus
Function / homology
Function and homology information


symbiont-mediated suppression of host transcription initiation from RNA polymerase II promoter / host cell nuclear membrane / IPs transport between nucleus and cytosol / IP3 and IP4 transport between cytosol and nucleus / IP6 and IP7 transport between cytosol and nucleus / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / telomere tethering at nuclear periphery / nuclear pore complex assembly / nuclear pore outer ring / nuclear pore organization ...symbiont-mediated suppression of host transcription initiation from RNA polymerase II promoter / host cell nuclear membrane / IPs transport between nucleus and cytosol / IP3 and IP4 transport between cytosol and nucleus / IP6 and IP7 transport between cytosol and nucleus / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / telomere tethering at nuclear periphery / nuclear pore complex assembly / nuclear pore outer ring / nuclear pore organization / nuclear pore cytoplasmic filaments / Nuclear Pore Complex (NPC) Disassembly / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear inclusion body / Transport of Ribonucleoproteins into the Host Nucleus / nuclear pore nuclear basket / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / SUMOylation of SUMOylation proteins / structural constituent of nuclear pore / Transport of Mature mRNA Derived from an Intronless Transcript / positive regulation of mRNA splicing, via spliceosome / NS1 Mediated Effects on Host Pathways / Rev-mediated nuclear export of HIV RNA / RNA export from nucleus / Nuclear import of Rev protein / SUMOylation of RNA binding proteins / NEP/NS2 Interacts with the Cellular Export Machinery / Transport of Mature mRNA derived from an Intron-Containing Transcript / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / nuclear localization sequence binding / Viral Messenger RNA Synthesis / SUMOylation of ubiquitinylation proteins / mitotic spindle pole / Vpr-mediated nuclear import of PICs / viral budding via host ESCRT complex / SUMOylation of DNA replication proteins / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / Regulation of HSF1-mediated heat shock response / nuclear pore / SUMOylation of DNA damage response and repair proteins / mRNA export from nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / nuclear periphery / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / protein import into nucleus / Resolution of Sister Chromatid Cohesion / SUMOylation of chromatin organization proteins / regulation of mitotic spindle organization / HCMV Late Events / symbiont-mediated suppression of host mRNA export from nucleus / ubiquitin binding / promoter-specific chromatin binding / molecular condensate scaffold activity / RHO GTPases Activate Formins / fibrillar center / ISG15 antiviral mechanism / HCMV Early Events / Separation of Sister Chromatids / nuclear envelope / nuclear membrane / snRNP Assembly / structural constituent of virion / microtubule binding / nuclear body / transcription coactivator activity / ribonucleoprotein complex / host cell cytoplasm / symbiont-mediated suppression of host gene expression / mRNA binding / viral envelope / SARS-CoV-2 activates/modulates innate and adaptive immune responses / virion membrane / RNA binding / nucleoplasm / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
Arc Repressor Mutant, subunit A - #2360 / VSV matrix protein / VSV matrix protein / Vesiculovirus matrix / VSV matrix superfamily / Vesiculovirus matrix protein / Nup98, Gle2-binding sequence / Nuclear pore complex protein NUP96, C-terminal domain / Nuclear protein 96 / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain ...Arc Repressor Mutant, subunit A - #2360 / VSV matrix protein / VSV matrix protein / Vesiculovirus matrix / VSV matrix superfamily / Vesiculovirus matrix protein / Nup98, Gle2-binding sequence / Nuclear pore complex protein NUP96, C-terminal domain / Nuclear protein 96 / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain superfamily / Nucleoporin peptidase S59-like / Nup98-96 autopeptidase S59 / NUP C-terminal domain profile. / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Arc Repressor Mutant, subunit A / WD domain, G-beta repeat / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Roll / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Nuclear pore complex protein Nup98-Nup96 / mRNA export factor RAE1 / Matrix protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Vesicular stomatitis Indiana virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.15 Å
AuthorsRen, Y. / Quan, B. / Seo, H.S. / Blobel, G.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1 Nup98).
Authors: Quan, B. / Seo, H.S. / Blobel, G. / Ren, Y.
History
DepositionFeb 3, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 25, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2014Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Other / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Mar 21, 2018Group: Data collection / Category: diffrn_detector / Item: _diffrn_detector.pdbx_collection_date
Revision 1.4Nov 20, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Dec 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / refine_hist
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.number_atoms_solvent / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: mRNA export factor
B: Nuclear pore complex protein Nup98-Nup96
C: Matrix protein


Theoretical massNumber of molelcules
Total (without water)66,0963
Polymers66,0963
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5250 Å2
ΔGint-14 kcal/mol
Surface area24840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)141.372, 141.372, 78.462
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number90
Space group name H-MP4212

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Components

#1: Protein mRNA export factor / Rae1 protein homolog / mRNA-associated protein mrnp 41


Mass: 38093.949 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAE1, MRNP41 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P78406
#2: Protein Nuclear pore complex protein Nup98-Nup96


Mass: 6514.310 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NUP98, ADAR2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P52948
#3: Protein Matrix protein


Mass: 21487.424 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vesicular stomatitis Indiana virus / Strain: 85CLB South America / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q8B0H7

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.97 Å3/Da / Density % sol: 58.53 %
Crystal growTemperature: 298 K / Method: vapor diffusion / Details: 0.1 M HEPES pH 7.5, 11% PEG 10, 000, and 10% MPD

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 13, 2012
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 3.15→30 Å / Num. obs: 14247 / % possible obs: 97.2 % / Redundancy: 5 % / Net I/σ(I): 15.5

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Processing

SoftwareName: REFMAC / Version: 5.5.0109 / Classification: refinement
RefinementResolution: 3.15→29.32 Å / Cor.coef. Fo:Fc: 0.906 / Cor.coef. Fo:Fc free: 0.824 / SU B: 23.81 / SU ML: 0.409 / Cross valid method: THROUGHOUT / ESU R Free: 0.56 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.28889 666 5 %RANDOM
Rwork0.21302 ---
obs0.21671 12717 93.94 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 46.907 Å2
Baniso -1Baniso -2Baniso -3
1--0.12 Å20 Å20 Å2
2---0.12 Å20 Å2
3---0.24 Å2
Refinement stepCycle: 1 / Resolution: 3.15→29.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4471 0 0 0 4471
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0224595
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0671.9356225
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9085555
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.41623.843216
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.45115760
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.981525
X-RAY DIFFRACTIONr_chiral_restr0.0740.2655
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0213537
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6322804
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.14734535
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.4862.51791
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.8163.51690
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3.15→3.231 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.372 36 -
Rwork0.256 736 -
obs--76.36 %

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