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- PDB-7eyj: Crystal structure of Escherichia coli ppnP -

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Basic information

Entry
Database: PDB / ID: 7eyj
TitleCrystal structure of Escherichia coli ppnP
ComponentsPyrimidine/purine nucleoside phosphorylase
KeywordsHYDROLASE / Pyrimidine / purine / nucleoside phosphorylase
Function / homology
Function and homology information


pyrimidine-nucleoside phosphorylase activity / pyrimidine-nucleoside phosphorylase / thymidine phosphorylase activity / deoxyuridine phosphorylase activity / uridine phosphorylase activity / guanosine phosphorylase activity / purine-nucleoside phosphorylase / purine-nucleoside phosphorylase activity / protein homodimerization activity / cytosol
Similarity search - Function
Pyrimidine/purine nucleoside phosphorylase / Pyrimidine/purine nucleoside phosphorylase / RmlC-like cupin domain superfamily / RmlC-like jelly roll fold
Similarity search - Domain/homology
Pyrimidine/purine nucleoside phosphorylase
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.38 Å
AuthorsWen, Y. / Wu, B.X.
CitationJournal: Proteins / Year: 2022
Title: Crystal structures of a new class of pyrimidine/purine nucleoside phosphorylase revealed a Cupin fold.
Authors: Wen, Y. / Li, X. / Guo, W. / Wu, B.
History
DepositionMay 31, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 9, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 23, 2022Group: Database references / Category: citation / Item: _citation.title
Revision 1.2May 4, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: Pyrimidine/purine nucleoside phosphorylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,4232
Polymers10,3271
Non-polymers961
Water2,270126
1
A: Pyrimidine/purine nucleoside phosphorylase
hetero molecules

A: Pyrimidine/purine nucleoside phosphorylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8474
Polymers20,6552
Non-polymers1922
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_455-x-1,-y,z1
Buried area2220 Å2
ΔGint-30 kcal/mol
Surface area9210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.892, 59.892, 52.145
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number171
Space group name H-MP62
Space group name HallP62
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/3
#3: y,-x+y,z+2/3
#4: -y,x-y,z+2/3
#5: -x+y,-x,z+1/3
#6: -x,-y,z

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Components

#1: Protein Pyrimidine/purine nucleoside phosphorylase / Adenosine phosphorylase / Cytidine phosphorylase / Guanosine phosphorylase / Inosine phosphorylase ...Adenosine phosphorylase / Cytidine phosphorylase / Guanosine phosphorylase / Inosine phosphorylase / Thymidine phosphorylase / Uridine phosphorylase / Xanthosine phosphorylase


Mass: 10327.409 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K-12 / Gene: ppnP / Production host: Escherichia coli (E. coli) / References: UniProt: P0C037
#2: Chemical ChemComp-SO4 / SULFATE ION


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


Mass: 18.015 Da / Num. of mol.: 126 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.61 Å3/Da / Density % sol: 52.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 2.0 M Ammonium sulfate (dibasic),0.1M CAPS/Sodium hydroxide pH 10.5, 0.2M Lithium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97915 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 27, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97915 Å / Relative weight: 1
ReflectionResolution: 1.38→50 Å / Num. obs: 21996 / % possible obs: 99.9 % / Redundancy: 19.9 % / CC1/2: 0.987 / CC star: 0.997 / Rmerge(I) obs: 0.084 / Rpim(I) all: 0.019 / Net I/σ(I): 37.3
Reflection shellResolution: 1.38→1.43 Å / Rmerge(I) obs: 0.196 / Mean I/σ(I) obs: 18.7 / Num. unique obs: 2189 / CC1/2: 0.989 / CC star: 0.997 / Rpim(I) all: 0.046

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Processing

Software
NameVersionClassification
REFMACv1.0refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: SAD / Resolution: 1.38→20 Å / Cross valid method: FREE R-VALUE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.178 1071 4.91 %
Rwork0.1522 --
obs0.1534 21825 99.2 %
Displacement parametersBiso mean: 15.61 Å2
Refinement stepCycle: LAST / Resolution: 1.38→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms726 0 5 126 857
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0052785
X-RAY DIFFRACTIONf_angle_d0.86671074
X-RAY DIFFRACTIONf_chiral_restr0.0926118
X-RAY DIFFRACTIONf_plane_restr0.0054141
X-RAY DIFFRACTIONf_dihedral_angle_d15.3956460

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