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- PDB-2kei: Refined Solution Structure of a Dimer of LAC repressor DNA-Bindin... -

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Basic information

Entry
Database: PDB / ID: 2kei
TitleRefined Solution Structure of a Dimer of LAC repressor DNA-Binding domain complexed to its natural operator O1
Components
  • DNA (5'-D(*GP*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*GP*GP*AP*TP*AP*AP*CP*AP*AP*TP*TP*T)-3')
  • DNA (5'-D(P*AP*AP*AP*TP*TP*GP*TP*TP*AP*TP*CP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*TP*C)-3')
  • Lactose operon repressor
KeywordsTranscription/DNA / Lac repressor / lac operators / protein-DNA complex / DNA-binding / Repressor / Transcription / Transcription regulation / Transcription-DNA COMPLEX
Function / homology
Function and homology information


DNA-binding transcription repressor activity / cis-regulatory region sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / identical protein binding / cytosol
Similarity search - Function
LacI-type HTH domain signature. / Transcriptional regulator LacI/GalR-like, sensor domain / Periplasmic binding protein-like domain / LacI-type HTH domain / Bacterial regulatory proteins, lacI family / LacI-type HTH domain profile. / helix_turn _helix lactose operon repressor / lambda repressor-like DNA-binding domains / 434 Repressor (Amino-terminal Domain) / Lambda repressor-like, DNA-binding domain superfamily ...LacI-type HTH domain signature. / Transcriptional regulator LacI/GalR-like, sensor domain / Periplasmic binding protein-like domain / LacI-type HTH domain / Bacterial regulatory proteins, lacI family / LacI-type HTH domain profile. / helix_turn _helix lactose operon repressor / lambda repressor-like DNA-binding domains / 434 Repressor (Amino-terminal Domain) / Lambda repressor-like, DNA-binding domain superfamily / Periplasmic binding protein-like I / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA / DNA (> 10) / Lactose operon repressor
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
AuthorsRomanuka, J. / Folkers, G. / Biris, N. / Tishchenko, E. / Wienk, H. / Kaptein, R. / Boelens, R.
CitationJournal: J.Mol.Biol. / Year: 2009
Title: Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes.
Authors: Romanuka, J. / Folkers, G.E. / Biris, N. / Tishchenko, E. / Wienk, H. / Bonvin, A.M. / Kaptein, R. / Boelens, R.
History
DepositionJan 30, 2009Deposition site: BMRB / Processing site: RCSB
Revision 1.0May 19, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 20, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Lactose operon repressor
B: Lactose operon repressor
C: DNA (5'-D(*GP*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*GP*GP*AP*TP*AP*AP*CP*AP*AP*TP*TP*T)-3')
D: DNA (5'-D(P*AP*AP*AP*TP*TP*GP*TP*TP*AP*TP*CP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*TP*C)-3')


Theoretical massNumber of molelcules
Total (without water)27,7644
Polymers27,7644
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Lactose operon repressor


Mass: 6822.755 Da / Num. of mol.: 2 / Fragment: UNP residues 1-62 / Mutation: V52C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Gene: lacI, b0345, JW0336 / Production host: Escherichia coli (E. coli) / Strain (production host): DH9 / References: UniProt: P03023
#2: DNA chain DNA (5'-D(*GP*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*GP*GP*AP*TP*AP*AP*CP*AP*AP*TP*TP*T)-3')


Mass: 7143.645 Da / Num. of mol.: 1 / Source method: obtained synthetically
#3: DNA chain DNA (5'-D(P*AP*AP*AP*TP*TP*GP*TP*TP*AP*TP*CP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*TP*C)-3')


Mass: 6974.534 Da / Num. of mol.: 1 / Source method: obtained synthetically

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-13C NOESY
1213D 1H-15N NOESY
1312D 1H-1H NOESY

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Sample preparation

DetailsContents: 2 mM DNA (5'-D(*DGP*DAP*DAP*DTP*DTP*DGP*DTP*DGP*DAP*DGP*DCP*DGP*DGP*DAP*DTP*DAP*DAP*DCP*DAP*DAP*DTP*DTP*DT)-3'), 2 mM DNA (5'- ...Contents: 2 mM DNA (5'-D(*DGP*DAP*DAP*DTP*DTP*DGP*DTP*DGP*DAP*DGP*DCP*DGP*DGP*DAP*DTP*DAP*DAP*DCP*DAP*DAP*DTP*DTP*DT)-3'), 2 mM DNA (5'-D(P*DAP*DAP*DAP*DTP*DTP*DGP*DTP*DTP*DAP*DTP*DCP*DCP*DGP*DCP*DTP*DCP*DAP*DCP*DAP*DAP*DTP*DTP*DC)-3'), 2 mM Lac headpiece dimer, 10% D2O, 10 mM potassium phosphate, 20 mM potassium chloride, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
2 mMDNA (5'-D(*DGP*DAP*DAP*DTP*DTP*DGP*DTP*DGP*DAP*DGP*DCP*DGP*DGP*DAP*DTP*DAP*DAP*DCP*DAP*DAP*DTP*DTP*DT)-3')1
2 mMDNA (5'-D(P*DAP*DAP*DAP*DTP*DTP*DGP*DTP*DTP*DAP*DTP*DCP*DCP*DGP*DCP*DTP*DCP*DAP*DCP*DAP*DAP*DTP*DTP*DC)-3')1
2 mMLac headpiece dimer1
10 %D2O-1
10 mMpotassium phosphate1
20 mMpotassium chloride1
Sample conditionsIonic strength: 0.03 / pH: 6 / Pressure: ambient / Temperature: 315 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX7501
Bruker DRXBrukerDRX6002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.2Brunger, Adams, Clore, Gros, Nilges and Readrefinement
XwinNMRBruker Biospinchemical shift assignment
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
HADDOCK2.1Dominguez, Boelens, Bonvinrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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