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- PDB-6jvx: Crystal structure of RBM38 in complex with RNA -

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Basic information

Entry
Database: PDB / ID: 6jvx
TitleCrystal structure of RBM38 in complex with RNA
Components
  • RNA (5'-R(*UP*GP*UP*GP*UP*GP*UP*GP*UP*GP*UP*G)-3')
  • RNA-binding protein 38
KeywordsRNA BINDING PROTEIN/RNA / RBM38 / RNA binding / Translational regulation / RNA BINDING PROTEIN / RNA BINDING PROTEIN-RNA complex
Function / homology
Function and homology information


regulation of myotube differentiation / DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / 3'-UTR-mediated mRNA stabilization / regulation of RNA splicing / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / RNA splicing / mRNA 3'-UTR binding / mRNA processing / cell differentiation / regulation of cell cycle ...regulation of myotube differentiation / DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / 3'-UTR-mediated mRNA stabilization / regulation of RNA splicing / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / RNA splicing / mRNA 3'-UTR binding / mRNA processing / cell differentiation / regulation of cell cycle / cell cycle / negative regulation of cell population proliferation / mRNA binding / RNA binding / nucleus / cytosol
Similarity search - Function
RRM (RNA recognition motif) domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
RNA / RNA (> 10) / RNA-binding protein 38
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.301 Å
AuthorsQian, K. / Li, M. / Wang, J. / Zhang, M. / Wang, M.
CitationJournal: Biochem.J. / Year: 2020
Title: Structural basis for mRNA recognition by human RBM38.
Authors: Qian, K. / Li, M. / Wang, J. / Zhang, M. / Wang, M.
History
DepositionApr 17, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 1, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 29, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2Nov 22, 2023Group: 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: RNA-binding protein 38
B: RNA (5'-R(*UP*GP*UP*GP*UP*GP*UP*GP*UP*GP*UP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,9094
Polymers17,7172
Non-polymers1922
Water2,288127
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1970 Å2
ΔGint-38 kcal/mol
Surface area6080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.809, 78.809, 66.982
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121

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Components

#1: Protein RNA-binding protein 38 / CLL-associated antigen KW-5 / HSRNASEB / RNA-binding motif protein 38 / RNA-binding region- ...CLL-associated antigen KW-5 / HSRNASEB / RNA-binding motif protein 38 / RNA-binding region-containing protein 1 / ssDNA-binding protein SEB4


Mass: 13853.546 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBM38, RNPC1, SEB4 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H0Z9
#2: RNA chain RNA (5'-R(*UP*GP*UP*GP*UP*GP*UP*GP*UP*GP*UP*G)-3')


Mass: 3863.272 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 127 / Source method: isolated from a natural source / Formula: H2O

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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: 3.39 Å3/Da / Density % sol: 63.71 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 0.1M Tris-HCl (pH8.0), 2M ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9791 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 15, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 10894 / % possible obs: 98.9 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.101 / Rpim(I) all: 0.049 / Rrim(I) all: 0.113 / Χ2: 1.049 / Net I/σ(I): 9.8 / Num. measured all: 53598
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.3-2.3850.94210750.6790.4681.0571.09499.1
2.38-2.484.80.67910640.7240.3420.7651.05698.7
2.48-2.594.80.46610590.8580.2290.5221.08298.7
2.59-2.735.20.36110980.9320.1740.4031.05899.8
2.73-2.95.20.24310730.9680.1160.2711.06399.9
2.9-3.125.10.14410930.9880.0680.161.00899.8
3.12-3.444.90.09910890.9920.0480.111.0299.3
3.44-3.934.70.07510740.9950.0360.0831.02297.1
3.93-4.9550.06111180.9950.0290.0680.988100
4.95-504.60.05811510.9960.0280.0651.10597.1

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Processing

Software
NameVersionClassification
HKL-2000data reduction
HKL-2000data scaling
PHENIX1.14_3260refinement
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2cqd
Resolution: 2.301→39.405 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 23.37
RfactorNum. reflection% reflection
Rfree0.2205 524 4.82 %
Rwork0.1775 --
obs0.1795 10876 98.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 128.63 Å2 / Biso mean: 43.1122 Å2 / Biso min: 15.44 Å2
Refinement stepCycle: final / Resolution: 2.301→39.405 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms670 153 10 127 960
Biso mean--69.6 49.04 -
Num. residues----95
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3014-2.5330.3361340.26562530266499
2.533-2.89950.24021350.206825672702100
2.8995-3.65260.18971200.15952578269899
3.6526-39.41030.19841350.15582677281299
Refinement TLS params.Method: refined / Origin x: -30.1613 Å / Origin y: 25.7511 Å / Origin z: 4.679 Å
111213212223313233
T0.1881 Å2-0.022 Å2-0.0209 Å2-0.1809 Å20.0187 Å2--0.2115 Å2
L4.982 °22.7382 °20.7568 °2-4.394 °21.0372 °2--5.1837 °2
S-0.2635 Å °-0.0755 Å °-0.032 Å °-0.2416 Å °0.1664 Å °0.1162 Å °0.2879 Å °-0.1764 Å °0.1078 Å °
Refinement TLS groupSelection details: (chain 'A' and resid 29 through 115)

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