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- PDB-1wcn: NMR structure of the carboxyterminal domains of Escherichia coli NusA -

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Basic information

Entry
Database: PDB / ID: 1wcn
TitleNMR structure of the carboxyterminal domains of Escherichia coli NusA
ComponentsTRANSCRIPTION ELONGATION PROTEIN NUSA
KeywordsRNA BINDING PROTEIN / RNA-BINDING PROTEIN / ESCHERICHIA COLI NUSA / TRANSCRIPTION REGULATION / REGULATION OF RNA BINDING / TRANSCRIPTION ANTITERMINATION AND TERMINATION / C-TERMINAL REPEAT UNITS / RNA-BINDING
Function / homology
Function and homology information


bacterial-type RNA polymerase core enzyme binding / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription termination / ribosome biogenesis / protein complex oligomerization / DNA-binding transcription factor activity / protein domain specific binding / nucleotide binding ...bacterial-type RNA polymerase core enzyme binding / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription termination / ribosome biogenesis / protein complex oligomerization / DNA-binding transcription factor activity / protein domain specific binding / nucleotide binding / RNA binding / cytosol / cytoplasm
Similarity search - Function
Transcription termination factor NusA, C-terminal duplication / Transcription termination factor NusA / Transcription factor NusA, N-terminal / KH domain, NusA-like / NusA, N-terminal domain superfamily / NusA N-terminal domain / NusA-like KH domain / Transcription termination/antitermination protein NusA, bacterial / RNA-binding domain, S1 / Type-1 KH domain profile. ...Transcription termination factor NusA, C-terminal duplication / Transcription termination factor NusA / Transcription factor NusA, N-terminal / KH domain, NusA-like / NusA, N-terminal domain superfamily / NusA N-terminal domain / NusA-like KH domain / Transcription termination/antitermination protein NusA, bacterial / RNA-binding domain, S1 / Type-1 KH domain profile. / DNA repair Rad51/transcription factor NusA, alpha-helical / Helix-hairpin-helix domain / S1 domain profile. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / S1 domain / 5' to 3' exonuclease, C-terminal subdomain / DNA polymerase; domain 1 / K homology domain superfamily, prokaryotic type / K homology domain-like, alpha/beta / Nucleic acid-binding, OB-fold / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Transcription termination/antitermination protein NusA / Transcription termination/antitermination protein NusA
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
MethodSOLUTION NMR / MANUAL
AuthorsEisenmann, A. / Schwarz, S. / Schweimer, K. / Roesch, P.
CitationJournal: Protein Sci. / Year: 2005
Title: The E. Coli Nusa Carboxy-Terminal Domains are Structurally Similar and Show Specific Rnap- and Lambdan Interactions
Authors: Eisenmann, A. / Schwarz, S. / Prasch, S. / Schweimer, K. / Roesch, P.
History
DepositionNov 18, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 31, 2005Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRANSCRIPTION ELONGATION PROTEIN NUSA


Theoretical massNumber of molelcules
Total (without water)7,4691
Polymers7,4691
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)19 / 90LEAST RESTRAINT VIOLATION
RepresentativeModel #1

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Components

#1: Protein TRANSCRIPTION ELONGATION PROTEIN NUSA / N UTILIZATION SUBSTANCE PROTEIN A / L FACTOR NUSA


Mass: 7469.270 Da / Num. of mol.: 1 / Fragment: ACIDIC REPEAT 2, RESIDUES 426-495
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PTKK19 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03003, UniProt: P0AFF6*PLUS
Compound detailsFUNCTION: PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION OF TRANSCRIPTION. NUSA BINDS ...FUNCTION: PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION OF TRANSCRIPTION. NUSA BINDS DIRECTLY TO THE CORE ENZYME OF THE DNA-DEPENDENT RNA POLYMERASE. NUSA ALSO INTERACTS WITH LAMBDA N PROTEIN, RNA, RHO FACTOR, AND PERHAPS NUSB. BINDS RNA.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: SEE PUBLICATION
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N LABELED GP-NUSA(339-495)

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Sample preparation

DetailsContents: 90% WATER / 10% D2O
Sample conditionsIonic strength: 50 mM / pH: 6.8 / Pressure: 1.0 atm / Temperature: 298.0 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Xplor-NIH1.2.1SCHWIETERS, KUSZEWSKI, TJrefinement
NMRViewstructure solution
RefinementMethod: MANUAL / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JOURNAL CITATION ABOVE
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 90 / Conformers submitted total number: 19

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