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- PDB-1opi: SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2... -

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Entry
Database: PDB / ID: 1opi
TitleSOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE
Components
  • SPLICING FACTOR SF1
  • SPLICING FACTOR U2AF 65 KDA SUBUNIT
KeywordsRNA BINDING PROTEIN / NON-CANONICAL RNA RECOGNITION MOTIF / 4-STRANDED ANTI-PARALLEL BETA-SHEET / 2 ALPHA HELICES ADDITIONALLY EXTENDED BY A THIRD HELIX C
Function / homology
Function and homology information


U2AF complex / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / mRNA 3'-end processing / C2H2 zinc finger domain binding / regulation of mRNA splicing, via spliceosome / commitment complex / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / U2-type prespliceosome ...U2AF complex / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / mRNA 3'-end processing / C2H2 zinc finger domain binding / regulation of mRNA splicing, via spliceosome / commitment complex / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / U2-type prespliceosome / molecular function inhibitor activity / spliceosomal complex assembly / mRNA 3'-splice site recognition / negative regulation of mRNA splicing, via spliceosome / Protein hydroxylation / negative regulation of protein ubiquitination / mRNA Splicing - Major Pathway / positive regulation of RNA splicing / spliceosomal complex / negative regulation of smooth muscle cell proliferation / mRNA splicing, via spliceosome / mRNA processing / transcription corepressor activity / nuclear speck / ribosome / mRNA binding / enzyme binding / RNA binding / zinc ion binding / nucleoplasm / identical protein binding / nucleus
Similarity search - Function
Splicing factor 1, helix-hairpin domain / : / Splicing factor 1 helix-hairpin domain / : / KHDC4/BBP-like, KH-domain type I / KH domain-containing BBP-like / U2 snRNP auxilliary factor, large subunit, splicing factor / Type-1 KH domain profile. / K Homology domain, type 1 superfamily / RRM (RNA recognition motif) domain ...Splicing factor 1, helix-hairpin domain / : / Splicing factor 1 helix-hairpin domain / : / KHDC4/BBP-like, KH-domain type I / KH domain-containing BBP-like / U2 snRNP auxilliary factor, large subunit, splicing factor / Type-1 KH domain profile. / K Homology domain, type 1 superfamily / 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 / K Homology domain / K homology RNA-binding domain / zinc finger / Zinc knuckle / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Splicing factor U2AF 65 kDa subunit / Splicing factor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS USING CNS, ARIA FOR AMBIGUOUS DISTANCE RESTRAINTS
AuthorsSelenko, P. / Gregorovic, G. / Sprangers, R. / Stier, G. / Rhani, Z. / Kramer, A. / Sattler, M.
CitationJournal: Mol.Cell / Year: 2003
Title: Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
Authors: Selenko, P. / Gregorovic, G. / Sprangers, R. / Stier, G. / Rhani, Z. / Kramer, A. / Sattler, M.
History
DepositionMar 5, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: SPLICING FACTOR U2AF 65 KDA SUBUNIT
B: SPLICING FACTOR SF1


Theoretical massNumber of molelcules
Total (without water)13,6692
Polymers13,6692
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS, STRUCTURES WITH THE LOWEST ENERGY
RepresentativeModel #1lowest energy

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Components

#1: Protein SPLICING FACTOR U2AF 65 KDA SUBUNIT / U2 AUXILIARY FACTOR 65 KDA SUBUNIT / U2 SNRNP AUXILIARY FACTOR LARGE SUBUNIT / HU2AF(65)


Mass: 11976.615 Da / Num. of mol.: 1 / Fragment: C-TERMINAL RRM DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: MODIFIED PET24D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: P26368
#2: Protein/peptide SPLICING FACTOR SF1


Mass: 1691.936 Da / Num. of mol.: 1 / Fragment: N-TERMINAL PEPTIDE / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED AND DERIVED FROM THE N-TERMINUS OF SF1. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
References: UniProt: Q15637

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-SEPARATED NOESY
1213D 15N-SEPARATED NOESY
1313D 13C/15N-EDITED/FILTERED NOESY

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Sample preparation

DetailsContents: 1MM 15N,13C U2AF65-RRM3 + 1MM UNLABELED SF1_10-25, 30MM PHOSPHATE BUFFER, 20MM NACL, 3MM DTT
Solvent system: D2O
Sample conditionsIonic strength: 50mM SALT / pH: 6.4 / Pressure: AMBIENT / Temperature: 295 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX5002
Bruker DRXBrukerDRX8003

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1BRUNGERrefinement
ARIA1.2NILGESrefinement
RefinementMethod: RESTRAINED MOLECULAR DYNAMICS USING CNS, ARIA FOR AMBIGUOUS DISTANCE RESTRAINTS
Software ordinal: 1
Details: REFINEMENT OF PROTEIN STRUCTURES IN WATER SOLVENT, ACCORDING TO LINGE ET AL. (PROTEINS 50:496 -506, 2003)
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS, STRUCTURES WITH THE LOWEST ENERGY
Conformers calculated total number: 100 / Conformers submitted total number: 10

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