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- PDB-6f7s: Crystal structure of Human ARS2 residues 147-270 + 408-763 with d... -

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Basic information

Entry
Database: PDB / ID: 6f7s
TitleCrystal structure of Human ARS2 residues 147-270 + 408-763 with deletion of loop B
Components
  • Serrate RNA effector molecule homolog
  • Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog
KeywordsRNA BINDING PROTEIN
Function / homology
Function and homology information


mRNA cap binding complex binding / neuronal stem cell population maintenance / primary miRNA processing / response to arsenic-containing substance / positive regulation of neurogenesis / RNA polymerase II transcribes snRNA genes / mRNA Splicing - Major Pathway / mRNA processing / protein-macromolecule adaptor activity / nuclear body ...mRNA cap binding complex binding / neuronal stem cell population maintenance / primary miRNA processing / response to arsenic-containing substance / positive regulation of neurogenesis / RNA polymerase II transcribes snRNA genes / mRNA Splicing - Major Pathway / mRNA processing / protein-macromolecule adaptor activity / nuclear body / ribonucleoprotein complex / regulation of DNA-templated transcription / protein-containing complex / DNA binding / RNA binding / nucleoplasm / cytoplasm
Similarity search - Function
SERRATE/Ars2 , C-terminal / SERRATE/Ars2, N-terminal / SERRATE/Ars2 / Arsenite-resistance protein 2 / SERRATE/Ars2, N-terminal domain / RNA-binding domain superfamily
Similarity search - Domain/homology
Serrate RNA effector molecule homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.37 Å
AuthorsCusack, S. / Schulze, W.M.
Funding support France, 1items
OrganizationGrant numberCountry
European Research Council322586 France
CitationJournal: Nat Commun / Year: 2018
Title: Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting.
Authors: Schulze, W.M. / Stein, F. / Rettel, M. / Nanao, M. / Cusack, S.
History
DepositionDec 11, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 9, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Serrate RNA effector molecule homolog
C: Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog
B: Serrate RNA effector molecule homolog
D: Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog


Theoretical massNumber of molelcules
Total (without water)106,4804
Polymers106,4804
Non-polymers00
Water00
1
A: Serrate RNA effector molecule homolog
C: Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog


Theoretical massNumber of molelcules
Total (without water)53,2402
Polymers53,2402
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5880 Å2
ΔGint-36 kcal/mol
Surface area26750 Å2
MethodPISA
2
B: Serrate RNA effector molecule homolog
D: Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog


Theoretical massNumber of molelcules
Total (without water)53,2402
Polymers53,2402
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5790 Å2
ΔGint-39 kcal/mol
Surface area25470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.510, 148.270, 235.660
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1010A149 - 762
2010B149 - 762

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Components

#1: Protein Serrate RNA effector molecule homolog / Arsenite-resistance protein 2


Mass: 14754.771 Da / Num. of mol.: 2 / Fragment: UNP residues 147-270
Source method: isolated from a genetically manipulated source
Details: Residues 147-270 and 408-763 were co-expressed as separate pieces.Residues 271-407 were deleted.Residues 568-598 (denoted loop B) were replaced by GSGSGS
Source: (gene. exp.) Homo sapiens (human) / Gene: SRRT, ARS2, ASR2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 / References: UniProt: Q9BXP5
#2: Protein Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog / Arsenite-resistance protein 2


Mass: 38485.297 Da / Num. of mol.: 2 / Fragment: UNP residues 408-567,UNP residues 599-763
Source method: isolated from a genetically manipulated source
Details: Residues 147-270 and 408-763 were co-expressed as separate pieces.Residues 271-407 were deleted.Residues 568-598 (denoted loop B) were replaced by GSGSGS,Residues 147-270 and 408-763 were co- ...Details: Residues 147-270 and 408-763 were co-expressed as separate pieces.Residues 271-407 were deleted.Residues 568-598 (denoted loop B) were replaced by GSGSGS,Residues 147-270 and 408-763 were co-expressed as separate pieces.Residues 271-407 were deleted.Residues 568-598 (denoted loop B) were replaced by GSGSGS
Source: (gene. exp.) Homo sapiens (human) / Gene: SRRT, ARS2, ASR2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 / References: UniProt: Q9BXP5

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.51 Å3/Da / Density % sol: 64.94 %
Crystal growTemperature: 281 K / Method: vapor diffusion, hanging drop / pH: 8.3
Details: Crystals of human ARS2 were obtained at 4 C in 2 microliter hanging drops with a 1:1 ratio of protein solution (6 mg per ml in 20 mM HEPES, 300 mM NaCl, 2 mM tris(2-carboxyethyl)phosphine, ...Details: Crystals of human ARS2 were obtained at 4 C in 2 microliter hanging drops with a 1:1 ratio of protein solution (6 mg per ml in 20 mM HEPES, 300 mM NaCl, 2 mM tris(2-carboxyethyl)phosphine, pH 7.8) to crystallisation solution. The crystallisation solution was 0.2 M potassium citrate tribasic monohydrate, 20 % (w/v) PEG 3350.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.966 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 10, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.966 Å / Relative weight: 1
ReflectionResolution: 3.37→117.83 Å / Num. obs: 20293 / % possible obs: 94.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.12 % / CC1/2: 0.998 / Rsym value: 0.098 / Net I/σ(I): 12.62
Reflection shellResolution: 3.37→3.46 Å / Redundancy: 3.82 % / Mean I/σ(I) obs: 1.97 / CC1/2: 0.537 / Rsym value: 0.674 / % possible all: 67.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0189refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6F7J

6f7j


Resolution: 3.37→117.83 Å / Cor.coef. Fo:Fc: 0.9 / Cor.coef. Fo:Fc free: 0.862 / SU B: 38.314 / SU ML: 0.564 / Cross valid method: THROUGHOUT / ESU R Free: 0.647 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.30296 1017 5 %RANDOM
Rwork0.25753 ---
obs0.25963 19276 94.26 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 124.446 Å2
Baniso -1Baniso -2Baniso -3
1-5.73 Å20 Å2-0 Å2
2---4.22 Å20 Å2
3----1.51 Å2
Refinement stepCycle: 1 / Resolution: 3.37→117.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7149 0 0 0 7149
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0197313
X-RAY DIFFRACTIONr_bond_other_d0.0010.026962
X-RAY DIFFRACTIONr_angle_refined_deg0.9431.9699841
X-RAY DIFFRACTIONr_angle_other_deg0.813316163
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.0455857
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.52523.598378
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.926151413
X-RAY DIFFRACTIONr_dihedral_angle_4_deg9.8351574
X-RAY DIFFRACTIONr_chiral_restr0.0520.21056
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0217952
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021514
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_it2.06912.6173449
X-RAY DIFFRACTIONr_mcbond_other2.06912.6163448
X-RAY DIFFRACTIONr_mcangle_it3.70418.9194299
X-RAY DIFFRACTIONr_mcangle_other3.70318.9194300
X-RAY DIFFRACTIONr_scbond_it1.44612.7673863
X-RAY DIFFRACTIONr_scbond_other1.44612.7673864
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.73819.0765543
X-RAY DIFFRACTIONr_long_range_B_refined5.527940
X-RAY DIFFRACTIONr_long_range_B_other5.527940
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Number: 26256 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.06 Å / Weight position: 0.05

Dom-IDAuth asym-ID
1A
2B
LS refinement shellResolution: 3.374→3.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.434 51 -
Rwork0.383 988 -
obs--66.95 %

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