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- PDB-1ox7: Crystal structure of yeast cytosine deaminase apo-enzyme: inorgan... -

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Basic information

Entry
Database: PDB / ID: 1ox7
TitleCrystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound
ComponentsCytosine deaminase
KeywordsHYDROLASE / aminohydrolase
Function / homology
Function and homology information


cytidine metabolic process / diaminohydroxyphosphoribosylaminopyrimidine deaminase activity / cytosine deaminase / pyrimidine-containing compound salvage / : / cytosine deaminase activity / UMP salvage / cytosine metabolic process / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Cytidine and deoxycytidylate deaminase zinc-binding region / Cytidine Deaminase, domain 2 / Cytidine Deaminase; domain 2 / APOBEC/CMP deaminase, zinc-binding / Cytidine and deoxycytidylate deaminases zinc-binding region signature. / Cytidine and deoxycytidylate deaminase domain / Cytidine and deoxycytidylate deaminases domain profile. / Cytidine deaminase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.43 Å
AuthorsIreton, G.C. / Black, M.E. / Stoddard, B.L.
CitationJournal: Structure / Year: 2003
Title: The 1.14 a crystal structure of yeast Cytosine deaminase. Evolution of nucleotide salvage enzymes and implications for genetic chemotherapy.
Authors: Ireton, G.C. / Black, M.E. / Stoddard, B.L.
History
DepositionApr 1, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 19, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytosine deaminase
B: Cytosine deaminase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4817
Polymers36,1792
Non-polymers3025
Water6,756375
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3510 Å2
ΔGint-177 kcal/mol
Surface area12490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.491, 70.467, 71.941
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 Cytosine deaminase / Cytosine aminohydrolase


Mass: 18089.492 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: FCY1 OR YPR062W OR YP9499.17 / Plasmid: pET15b-(yCD) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-RIL (DE3) / References: UniProt: Q12178, cytosine deaminase
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 375 / Source method: isolated from a natural source / Formula: H2O

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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: 1.74 Å3/Da / Density % sol: 28.68 %
Crystal growTemperature: 277 K / Method: streak seeding / pH: 6.5
Details: PEG 8000, calcium acetate, sodium cacodylate, pH 6.5, streak seeding, temperature 277K
Crystal grow
*PLUS
Temperature: 4. ℃ / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
130 %PEG80001drop
20.2 Msodium acetate1drop
30.1 Msodium cacodylate1drop
410 mg/mlprotein1drop
522-25 %PEG80001reservoir
60.2 Msodium acetate1reservoir
70.1 Msodium cacodylate1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 16, 2002
RadiationMonochromator: double crystal Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.43→20 Å / Num. all: 98785 / Num. obs: 98785 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.4 % / Biso Wilson estimate: 9.6 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 27.4
Reflection shellResolution: 1.43→1.48 Å / Rmerge(I) obs: 0.165 / Mean I/σ(I) obs: 9.5 / Num. unique all: 9823 / % possible all: 99.7
Reflection
*PLUS
Rmerge(I) obs: 0.042
Reflection shell
*PLUS
% possible obs: 99.7 %

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Processing

Software
NameVersionClassification
CNS1.1refinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: SAD / Resolution: 1.43→19.83 Å / Rfactor Rfree error: 0.003 / Isotropic thermal model: RESTRAINED / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.179 4829 4.9 %RANDOM
Rwork0.163 ---
all0.163 97892 --
obs0.163 97892 98.8 %-
Solvent computationBsol: 49.5037 Å2 / ksol: 0.376664 e/Å3
Displacement parametersBiso mean: 10.8 Å2
Baniso -1Baniso -2Baniso -3
1--0.06 Å20 Å20 Å2
2---0.23 Å20 Å2
3---0.28 Å2
Refine analyzeLuzzati coordinate error free: 0.14 Å / Luzzati sigma a free: 0.07 Å
Refinement stepCycle: LAST / Resolution: 1.43→19.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2458 0 5 375 2838
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.4
X-RAY DIFFRACTIONc_dihedral_angle_d21.8
X-RAY DIFFRACTIONc_improper_angle_d0.84
X-RAY DIFFRACTIONc_mcbond_it0.881.5
X-RAY DIFFRACTIONc_mcangle_it1.262
X-RAY DIFFRACTIONc_scbond_it2.12
X-RAY DIFFRACTIONc_scangle_it2.632.5
LS refinement shellResolution: 1.43→1.52 Å / Rfactor Rfree error: 0.007 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.201 826 5.2 %
Rwork0.171 15111 -
obs--96.8 %
Xplor file
Refine-IDSerial noTopol file
X-RAY DIFFRACTION1PROTEIN.TOP
X-RAY DIFFRACTION2ION.TOP
X-RAY DIFFRACTION3WATER.TOP
Refinement
*PLUS
Lowest resolution: 20 Å / Num. reflection obs: 51872 / Num. reflection Rfree: 2594 / % reflection Rfree: 5 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.37
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg21.8
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.84

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