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- PDB-1enw: ELONGATION FACTOR TFIIS DOMAIN II -

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Basic information

Entry
Database: PDB / ID: 1enw
TitleELONGATION FACTOR TFIIS DOMAIN II
ComponentsTRANSCRIPTION ELONGATION FACTOR S-II
KeywordsTRANSCRIPTION / helix-bundle
Function / homology
Function and homology information


RNA polymerase II complex recruiting activity / regulation of mRNA 3'-end processing / TP53 Regulates Transcription of DNA Repair Genes / Formation of TC-NER Pre-Incision Complex / RNA polymerase II complex binding / Gap-filling DNA repair synthesis and ligation in TC-NER / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / transcription by RNA polymerase III / Dual incision in TC-NER / transcription elongation by RNA polymerase I ...RNA polymerase II complex recruiting activity / regulation of mRNA 3'-end processing / TP53 Regulates Transcription of DNA Repair Genes / Formation of TC-NER Pre-Incision Complex / RNA polymerase II complex binding / Gap-filling DNA repair synthesis and ligation in TC-NER / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / transcription by RNA polymerase III / Dual incision in TC-NER / transcription elongation by RNA polymerase I / positive regulation of RNA polymerase II transcription preinitiation complex assembly / tRNA transcription by RNA polymerase III / transcription antitermination / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-templated transcription / zinc ion binding / nucleus
Similarity search - Function
Transcription elongation factor S-II, central domain / Transcription elongation factor, TFIIS / Transcription elongation factor, IIS-type / Transcription factor S-II (TFIIS), central domain / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / TFIIS central domain profile. / Transcription elongation factor, TFIIS/CRSP70, N-terminal, sub-type / Domain in the N-terminus of transcription elongation factor S-II (and elsewhere) ...Transcription elongation factor S-II, central domain / Transcription elongation factor, TFIIS / Transcription elongation factor, IIS-type / Transcription factor S-II (TFIIS), central domain / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / TFIIS central domain profile. / Transcription elongation factor, TFIIS/CRSP70, N-terminal, sub-type / Domain in the N-terminus of transcription elongation factor S-II (and elsewhere) / TFIIS helical bundle-like domain / Transcription factor IIS, N-terminal / TFIIS N-terminal domain profile. / TFIIS/LEDGF domain superfamily / Cyclin A; domain 1 / Zinc finger TFIIS-type signature. / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Transcription elongation factor S-II
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / simulated annealing, molecular dynamics
AuthorsMorin, P.E. / Awrey, D.E. / Edwards, A.M. / Arrowsmith, C.H.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: Elongation factor TFIIS contains three structural domains: solution structure of domain II.
Authors: Morin, P.E. / Awrey, D.E. / Edwards, A.M. / Arrowsmith, C.H.
History
DepositionMar 21, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 12, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 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 1.4Dec 21, 2022Group: Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.details
Revision 1.5May 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: TRANSCRIPTION ELONGATION FACTOR S-II


Theoretical massNumber of molelcules
Total (without water)12,7321
Polymers12,7321
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)20 / 50structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein TRANSCRIPTION ELONGATION FACTOR S-II


Mass: 12732.339 Da / Num. of mol.: 1 / Fragment: DOMAIN II (RESIDUES 131-240)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Production host: Bacteria (eubacteria) / References: UniProt: P07273

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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
1323D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
12 mM TFIIS; 5mM phosphate buffer; 90% H2O, 10% D2O90% H2O/10% D2O
22 mM TFIIS; 5mM phosphate buffer; 99.996% D2O99.996% D2O
Sample conditionsIonic strength: 50 mM / pH: 6.5 / Pressure: ambient / Temperature: 270 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA6002

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipe1995Delaglioprocessing
X-PLOR3.851Brungerstructure solution
X-PLOR3.851Brungerrefinement
RefinementMethod: simulated annealing, molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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