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- PDB-5tn0: Solution Structure of the N-terminal DNA-binding domain of the ma... -

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Basic information

Entry
Database: PDB / ID: 5tn0
TitleSolution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis
ComponentsHTH-type transcriptional regulator SinR
KeywordsTRANSCRIPTION / biofilm formation
Function / homology
Function and homology information


sporulation resulting in formation of a cellular spore / protein dimerization activity / DNA-binding transcription factor activity / negative regulation of gene expression / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / DNA binding
Similarity search - Function
SinR repressor/SinI anti-repressor, dimerisation domain / SinR repressor/SinI anti-repressor, dimerisation domain superfamily / Anti-repressor SinI / Sin domain profile. / Helix-turn-helix / Helix-turn-helix XRE-family like proteins / Cro/C1-type HTH domain profile. / lambda repressor-like DNA-binding domains / Cro/C1-type helix-turn-helix domain / 434 Repressor (Amino-terminal Domain) ...SinR repressor/SinI anti-repressor, dimerisation domain / SinR repressor/SinI anti-repressor, dimerisation domain superfamily / Anti-repressor SinI / Sin domain profile. / Helix-turn-helix / Helix-turn-helix XRE-family like proteins / Cro/C1-type HTH domain profile. / lambda repressor-like DNA-binding domains / Cro/C1-type helix-turn-helix domain / 434 Repressor (Amino-terminal Domain) / Lambda repressor-like, DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
HTH-type transcriptional regulator SinR
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsDraughn, G.L. / Bobay, B.G. / Stowe, S.D. / Thompson, R.J. / Cavanagh, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)RO1-GM055769 United States
CitationJournal: J.Mol.Biol. / Year: 2019
Title: The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis.
Authors: Milton, M.E. / Draughn, G.L. / Bobay, B.G. / Stowe, S.D. / Olson, A.L. / Feldmann, E.A. / Thompson, R.J. / Myers, K.H. / Santoro, M.T. / Kearns, D.B. / Cavanagh, J.
History
DepositionOct 13, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 25, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 9, 2019Group: Data collection / Database references
Category: citation / citation_author ...citation / citation_author / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HTH-type transcriptional regulator SinR


Theoretical massNumber of molelcules
Total (without water)7,8481
Polymers7,8481
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area4200 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100structures with the lowest energy
RepresentativeModel #1lowest energy
DetailsMonomer as determined by gel filtration

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Components

#1: Protein HTH-type transcriptional regulator SinR


Mass: 7847.908 Da / Num. of mol.: 1 / Fragment: residues 1-69
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (strain 168) (bacteria)
Strain: 168 / Gene: sinR, flaD, sin, BSU24610 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P06533

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
123isotropic12D 1H-13C HSQC
132isotropic13D HNCA
142isotropic13D HN(CO)CA
152isotropic13D HNCO
1142isotropic13D HN(CA)CO
1132isotropic13D HN(CA)CB
1122isotropic13D CBCA(CO)NH
1111isotropic13D 1H-15N TOCSY
1102isotropic13D C(CO)NH
191isotropic13D 1H-15N NOESY
183isotropic13D 1H-13C NOESY

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution11 mM [U-15N] SinrN, 20 mM MES, 200 mM sodium chloride, 0.02 % sodium azide, 90% H2O/10% D2O15N_sample90% H2O/10% D2O
solution21 mM [U-13C; U-15N] SinrN, 20 mM MES, 200 mM sodium chloride, 0.02 % sodium azide, 90% H2O/10% D2O15N_13C_sample90% H2O/10% D2O
solution31 mM [U-13C; U-15N] SinRN, 20 mM MES, 200 mM sodium chloride, 0.02 % sodium azide, 100% D2O15N_13C_D2O_sample100% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMSinrN[U-15N]1
20 mMMESnatural abundance1
200 mMsodium chloridenatural abundance1
0.02 %sodium azidenatural abundance1
1 mMSinrN[U-13C; U-15N]2
20 mMMESnatural abundance2
200 mMsodium chloridenatural abundance2
0.02 %sodium azidenatural abundance2
1 mMSinRN[U-13C; U-15N]3
20 mMMESnatural abundance3
200 mMsodium chloridenatural abundance3
0.02 %sodium azidenatural abundance3
Sample conditionsIonic strength: 200 mM / Label: conditions_1 / pH: 6.0 / Pressure: 1 atm / Temperature: 293 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR software
NameVersionDeveloperClassification
NMRViewJohnson, One Moon Scientificchemical shift assignment
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
NMRViewJohnson, One Moon Scientificpeak picking
Amber14Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollmanrefinement
CYANA3Guntert, Mumenthaler and Wuthrichstructure calculation
RefinementMethod: simulated annealing / Software ordinal: 4
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 10

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