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- PDB-4e6e: Crystal structure of a putative cell division protein FtsZ (Tfu_1... -

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Basic information

Entry
Database: PDB / ID: 4e6e
TitleCrystal structure of a putative cell division protein FtsZ (Tfu_1113) from Thermobifida fusca YX-ER1 at 2.22 A resolution (PSI Community Target, van Wezel G.P.)
ComponentsCell division protein ftsZ
KeywordsCELL CYCLE / Cell division / tubulin homolog / GTP-binding / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
Function / homology
Function and homology information


FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / GTPase activity / GTP binding / metal ion binding / cytoplasm
Similarity search - Function
Cell division protein FtsZ / Cell division protein FtsZ, conserved site / Cell division protein FtsZ, C-terminal / FtsZ family, C-terminal domain / FtsZ protein signature 1. / FtsZ protein signature 2. / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / 60s Ribosomal Protein L30; Chain: A; / Tubulin/FtsZ family, C-terminal domain ...Cell division protein FtsZ / Cell division protein FtsZ, conserved site / Cell division protein FtsZ, C-terminal / FtsZ family, C-terminal domain / FtsZ protein signature 1. / FtsZ protein signature 2. / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / 60s Ribosomal Protein L30; Chain: A; / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Cell division protein FtsZ
Similarity search - Component
Biological speciesThermobifida fusca (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.12 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be Published
Title: Crystal structure of a putative cell division protein FtsZ (Tfu_1113) from Thermobifida fusca YX-ER1 at 2.22 A resolution (PSI Community Target, van Wezel G.P.)
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionMar 15, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 6, 2012Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2013Group: Database references / Structure summary
Revision 1.2Nov 15, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cell division protein ftsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5188
Polymers32,2531
Non-polymers2647
Water2,504139
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Cell division protein ftsZ
hetero molecules

A: Cell division protein ftsZ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,03516
Polymers64,5072
Non-polymers52814
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_556y,x,-z+11
Buried area3960 Å2
ΔGint-122 kcal/mol
Surface area25250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)80.573, 80.573, 92.454
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221
Components on special symmetry positions
IDModelComponents
11A-602-

MG

21A-708-

HOH

31A-711-

HOH

41A-784-

HOH

DetailsCRYSTAL PACKING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

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Components

#1: Protein Cell division protein ftsZ


Mass: 32253.324 Da / Num. of mol.: 1 / Fragment: UNP residues 1-313
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermobifida fusca (bacteria) / Strain: YX / Gene: Tfu_1113 / Plasmid: SpeedET / Production host: Escherichia coli (E. coli) / Strain (production host): PB1 / References: UniProt: Q47QW6
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 139 / Source method: isolated from a natural source / Formula: H2O
Sequence details1. THE CONSTRUCT (1-313) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE ...1. THE CONSTRUCT (1-313) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. 2. THIS GENE USES AN ALTERNATE INITIATION CODON THAT RESULTS IN A VALINE AT POSITION 1 WHEN EXPRESSED AS A FUSION WITH THE PURIFICATION TAG.

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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: 2.69 Å3/Da / Density % sol: 54.21 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 1.600M magnesium sulfate, 0.1M MES pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97895
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 8, 2011
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: 0.97895 Å / Relative weight: 1
ReflectionResolution: 2.12→40.286 Å / Num. obs: 20109 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 11.17 % / Biso Wilson estimate: 44.564 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 19.3 / Num. measured all: 224590
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.12-2.187.31.0232.210608144499.8
2.18-2.237.90.8132.711317142999.4
2.23-2.38.30.3276.211417136999.6
2.3-2.378.50.3645.3116141371100
2.37-2.458.40.2776.910944130299.8
2.45-2.5313.30.5237.9167351257100
2.53-2.6313.30.3899.9164271239100
2.63-2.7412.90.29412.315241118299.8
2.74-2.8611.60.23914.113201113499.9
2.86-313.90.16719.1152701099100
3-3.1613.70.11125.5141891034100
3.16-3.3513.40.096291321498699.9
3.35-3.5813.10.0833.212234931100
3.58-3.8712.40.0673910891878100
3.87-4.24110.05940.2882680299.5
4.24-4.7413.20.05350.39628731100
4.74-5.4712.70.05848.48221648100
5.47-6.711.90.06844.16771567100
6.7-9.4810.90.04749.9473943398.9
9.48-40.2911.40.04955309627299.1

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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: 2.12→28.226 Å / Cor.coef. Fo:Fc: 0.9561 / Cor.coef. Fo:Fc free: 0.9311 / Occupancy max: 1 / Occupancy min: 0.5 / 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. SULFATE (SO4), MAGNESIUM (MG) FROM CRYSTALLIZATION CONDITION AND CHLORIDE (CL) FROM THE PROTEIN BUFFER ARE MODELED INTO THE STRUCTURE 3. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5. SAD EXPERIMENTAL PHASES WERE USED AS RESTRAINTS DURING REFINEMENT.
RfactorNum. reflection% reflectionSelection details
Rfree0.2307 1017 5.08 %RANDOM
Rwork0.1946 ---
obs0.1963 20025 99.57 %-
Displacement parametersBiso max: 137.98 Å2 / Biso mean: 56.0102 Å2 / Biso min: 26.56 Å2
Baniso -1Baniso -2Baniso -3
1-1.8981 Å20 Å20 Å2
2--1.8981 Å20 Å2
3----3.7962 Å2
Refine analyzeLuzzati coordinate error obs: 0.394 Å
Refinement stepCycle: LAST / Resolution: 2.12→28.226 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2159 0 11 139 2309
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d1038SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes60HARMONIC2
X-RAY DIFFRACTIONt_gen_planes337HARMONIC5
X-RAY DIFFRACTIONt_it2210HARMONIC20
X-RAY DIFFRACTIONt_nbd0SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion306SEMIHARMONIC5
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_contact2626SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d2210HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg2999HARMONIC21.07
X-RAY DIFFRACTIONt_omega_torsion2.97
X-RAY DIFFRACTIONt_other_torsion2.75
LS refinement shellResolution: 2.12→2.23 Å / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.343 131 4.61 %
Rwork0.2821 2709 -
all0.2848 2840 -
obs--99.57 %
Refinement TLS params.Method: refined / Origin x: 19.3397 Å / Origin y: 17.685 Å / Origin z: 28.1574 Å
111213212223313233
T0.0203 Å20.1443 Å20.0782 Å2--0.1508 Å20.0378 Å2---0.0627 Å2
L1.4655 °2-0.0053 °2-0.3015 °2-1.6461 °20.5618 °2--1.7158 °2
S0.1253 Å °0.2025 Å °0.1616 Å °-0.4524 Å °-0.1611 Å °-0.0147 Å °0.0562 Å °-0.1234 Å °0.0357 Å °

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