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- PDB-5frv: crystal structure of the phenol-responsive sensory domain of the ... -

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Basic information

Entry
Database: PDB / ID: 5frv
Titlecrystal structure of the phenol-responsive sensory domain of the transcription activator PoxR in complex with 4-methylphenol (Cresol)
ComponentsPOSITIVE PHENOL-DEGRADATIVE GENE REGULATOR
KeywordsTRANSCRIPTION / PHENOL / POXR / DMPR / ENHANCER-BINDING PROTEIN / ACTIVATOR / ATPASE FAMILY
Function / homology
Function and homology information


sequence-specific DNA binding / regulation of DNA-templated transcription / ATP hydrolysis activity / ATP binding / identical protein binding / metal ion binding
Similarity search - Function
Activator of aromatic catabolism / Activator of aromatic catabolism / 4-vinyl reductase, 4VR / V4R domain / V4R / Sigma-54 interaction domain ATP-binding region A signature. / Sigma-54 interaction domain, conserved site / Sigma-54 interaction domain C-terminal part signature. / Sigma-54 interaction domain, ATP-binding site 2 / Sigma-54 interaction domain ATP-binding region B signature. ...Activator of aromatic catabolism / Activator of aromatic catabolism / 4-vinyl reductase, 4VR / V4R domain / V4R / Sigma-54 interaction domain ATP-binding region A signature. / Sigma-54 interaction domain, conserved site / Sigma-54 interaction domain C-terminal part signature. / Sigma-54 interaction domain, ATP-binding site 2 / Sigma-54 interaction domain ATP-binding region B signature. / Sigma-54 interaction domain, ATP-binding site 1 / Sigma-54 interaction domain profile. / Sigma-54 interaction domain / RNA polymerase sigma factor 54 interaction domain / NO signalling/Golgi transport ligand-binding domain superfamily / DNA binding HTH domain, Fis-type / Bacterial regulatory protein, Fis family / Homeobox-like domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
P-CRESOL / Positive phenol-degradative gene regulator
Similarity search - Component
Biological speciesCUPRIAVIDUS NECATOR (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 1.9 Å
AuthorsPatil, V.V. / Woo, E.J.
CitationJournal: Structure / Year: 2016
Title: Structural Analysis of the Phenol-Responsive Sensory Domain of the Transcription Activator Poxr
Authors: Patil, V.V. / Park, K.-H. / Lee, S.-G. / Woo, E.J.
History
DepositionDec 23, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 30, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2016Group: Database references
Revision 1.2Apr 20, 2016Group: Database references
Revision 1.3Oct 16, 2019Group: Data collection / Other / Category: pdbx_database_status / reflns_shell
Item: _pdbx_database_status.status_code_sf / _reflns_shell.Rmerge_I_obs

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: POSITIVE PHENOL-DEGRADATIVE GENE REGULATOR
B: POSITIVE PHENOL-DEGRADATIVE GENE REGULATOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,3376
Polymers46,9902
Non-polymers3474
Water2,198122
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5220 Å2
ΔGint-42.9 kcal/mol
Surface area15910 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.696, 70.491, 105.175
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein POSITIVE PHENOL-DEGRADATIVE GENE REGULATOR / POXR


Mass: 23495.096 Da / Num. of mol.: 2 / Fragment: PHENOL BINDING DOMAIN, RESIDUES 1-211
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CUPRIAVIDUS NECATOR (bacteria) / Variant: E2 / Plasmid: PET22B-CPD / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O84957
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-PCR / P-CRESOL / P-Cresol


Mass: 108.138 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H8O
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 122 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.84 Å3/Da / Density % sol: 33.22 % / Description: NONE

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Data collection

DiffractionMean temperature: 287 K
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 0.97934
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 1.5→50 Å / Num. obs: 56079 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 13.7 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 37.29
Reflection shellResolution: 1.5→1.53 Å / Redundancy: 12.3 % / Mean I/σ(I) obs: 0.43 / % possible all: 99.7

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Processing

SoftwareName: PHENIX / Version: (PHENIX.REFINE: 1.9_1692) / Classification: refinement
RefinementMethod to determine structure: MIR
Starting model: NONE

Resolution: 1.9→23.348 Å / SU ML: 0.22 / σ(F): 1.33 / Phase error: 32.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2719 969 3.6 %
Rwork0.2268 --
obs0.2284 27099 96.47 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.9→23.348 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3114 0 18 122 3254
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0083196
X-RAY DIFFRACTIONf_angle_d1.0864304
X-RAY DIFFRACTIONf_dihedral_angle_d16.1681170
X-RAY DIFFRACTIONf_chiral_restr0.044458
X-RAY DIFFRACTIONf_plane_restr0.005556
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-2.00010.40381340.3973667X-RAY DIFFRACTION97
2.0001-2.12540.30361430.25473836X-RAY DIFFRACTION100
2.1254-2.28930.36721370.2863677X-RAY DIFFRACTION96
2.2893-2.51950.34051360.26623583X-RAY DIFFRACTION94
2.5195-2.88350.30841370.23533765X-RAY DIFFRACTION98
2.8835-3.63070.22631420.20823841X-RAY DIFFRACTION98
3.6307-23.34980.22761400.1853761X-RAY DIFFRACTION93

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