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- PDB-4epz: Crystal structure of a transcription anti-terminator antagonist U... -

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Basic information

Entry
Database: PDB / ID: 4epz
TitleCrystal structure of a transcription anti-terminator antagonist UpxZ (BACUNI_04315) from Bacteroides uniformis ATCC 8492 at 1.68 A resolution
Componentstranscription anti-terminator antagonist UpxZ
KeywordsTRANSCRIPTION / transcription regulation / antagonist of transcription anti-termination / regulation of capsular polysaccharide synthesis / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
Function / homologyUpxZ / UpxZ family / UpxZ superfamily / UpxZ family of transcription anti-terminator antagonists / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / metal ion binding / Mainly Alpha / Transcriptional regulator
Function and homology information
Biological speciesBacteroides uniformis ATCC 8492 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.68 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of a transcription anti-terminator antagonist UpxZ (BACUNI_04315) from Bacteroides uniformis ATCC 8492 at 1.68 A resolution
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionApr 17, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 11, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Revision 1.2Jan 24, 2018Group: Database references / Category: citation_author / Item: _citation_author.name
Revision 1.3Feb 1, 2023Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: transcription anti-terminator antagonist UpxZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,4153
Polymers19,3351
Non-polymers802
Water4,846269
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)42.253, 81.110, 105.702
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-547-

HOH

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Components

#1: Protein transcription anti-terminator antagonist UpxZ


Mass: 19334.555 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacteroides uniformis ATCC 8492 (bacteria)
Strain: ATCC 8492 / Gene: BACUNI_04315 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: A7V9P0
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 269 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsTHE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.34 Å3/Da / Density % sol: 47.48 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 0.2M calcium acetate, 20.0% polyethylene glycol 3350, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97868
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 4, 2012
Details: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)
RadiationMonochromator: single crystal Si(111) bent / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97868 Å / Relative weight: 1
ReflectionResolution: 1.68→37.864 Å / Num. obs: 20732 / % possible obs: 97.9 % / Observed criterion σ(I): -3 / Redundancy: 4.29 % / Biso Wilson estimate: 24.297 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 11.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
1.68-1.744.530.6782.359225203898.1
1.74-1.810.5213.19145204297.8
1.81-1.890.38748662199797.7
1.89-1.990.24569000208398.3
1.99-2.120.15399449212698.4
2.12-2.280.11311.38453201998.4
2.28-2.510.08214.99037206797.6
2.51-2.870.06517.78785206898
2.87-3.610.04722.88585208197.4
3.61-37.860.0425.58638221197.1

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
PDB_EXTRACT3.1data extraction
SHELXphasing
SHARPphasing
XSCALEDecember 29, 2011data scaling
BUSTER-TNT2.10.0refinement
XDSdata reduction
SHELXDphasing
BUSTER2.10.0refinement
RefinementMethod to determine structure: SAD / Resolution: 1.68→37.864 Å / Cor.coef. Fo:Fc: 0.9568 / Cor.coef. Fo:Fc free: 0.951 / Occupancy max: 1 / Occupancy min: 0.2 / Cross valid method: THROUGHOUT / σ(F): 0
Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. THE SAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. CALCIUM IONS MODELED WERE PRESENT IN THE CRYSTALLIZATION CONDITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.1963 1064 5.14 %RANDOM
Rwork0.1681 ---
obs0.1695 20711 98.05 %-
Displacement parametersBiso max: 97.42 Å2 / Biso mean: 31.6026 Å2 / Biso min: 13.94 Å2
Baniso -1Baniso -2Baniso -3
1--1.9487 Å20 Å20 Å2
2---4.1054 Å20 Å2
3---6.0542 Å2
Refine analyzeLuzzati coordinate error obs: 0.198 Å
Refinement stepCycle: LAST / Resolution: 1.68→37.864 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1276 0 2 269 1547
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d733SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes58HARMONIC2
X-RAY DIFFRACTIONt_gen_planes214HARMONIC5
X-RAY DIFFRACTIONt_it1416HARMONIC20
X-RAY DIFFRACTIONt_nbd1SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion184SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact1965SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d1416HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg1936HARMONIC20.91
X-RAY DIFFRACTIONt_omega_torsion2.74
X-RAY DIFFRACTIONt_other_torsion2.88
LS refinement shellResolution: 1.68→1.77 Å / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.2582 186 6.19 %
Rwork0.2041 2819 -
all0.2073 3005 -
obs--98.05 %
Refinement TLS params.Method: refined / Origin x: 6.4148 Å / Origin y: 27.6774 Å / Origin z: 39.3014 Å
111213212223313233
T-0.0061 Å2-0.023 Å20.014 Å2--0.0576 Å20.0027 Å2---0.0651 Å2
L1.0852 °20.3428 °20.3537 °2-0.6132 °20.3747 °2--1.5426 °2
S-0.0422 Å °-0.0065 Å °0.0191 Å °-0.0458 Å °0.002 Å °-0.0321 Å °-0.3033 Å °0.0734 Å °0.0402 Å °
Refinement TLS groupSelection details: { A|2 - 161 }

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