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- PDB-7w1q: The structure of the Arabidopsis thaliana guanosine deaminase mut... -

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Basic information

Entry
Database: PDB / ID: 7w1q
TitleThe structure of the Arabidopsis thaliana guanosine deaminase mutant E82Q complexed with 2'-O-methylguanosine
ComponentsGuanosine deaminase
KeywordsHYDROLASE / deamination / GSDA / purine metabolism / plant protein
Function / homology
Function and homology information


guanosine deaminase / guanosine deaminase activity / purine nucleoside catabolic process / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Cytidine and deoxycytidylate deaminase zinc-binding region / 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
Similarity search - Domain/homology
O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE / Guanosine deaminase
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsXie, W. / Jia, Q. / Zeng, H.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31870782 China
CitationJournal: Int J Mol Sci / Year: 2022
Title: Substrate Specificity of GSDA Revealed by Cocrystal Structures and Binding Studies.
Authors: Jia, Q. / Zhang, J. / Zeng, H. / Tang, J. / Xiao, N. / Gao, S. / Li, H. / Xie, W.
History
DepositionNov 19, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 23, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 15, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Guanosine deaminase
D: Guanosine deaminase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,0826
Polymers34,1972
Non-polymers8854
Water2,306128
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology, PDBePISA
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4590 Å2
ΔGint-96 kcal/mol
Surface area12650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.244, 119.244, 39.010
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number169
Space group name H-MP61
Space group name HallP61
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/6
#3: y,-x+y,z+5/6
#4: -y,x-y,z+1/3
#5: -x+y,-x,z+2/3
#6: -x,-y,z+1/2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: LEU / End label comp-ID: LEU / Auth seq-ID: 29 - 184 / Label seq-ID: 1 - 156

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1(chain 'A' and (resid 29 through 184 or (resid 185...AA
2(chain 'D' and (resid 29 through 129 or (resid 130...DB

NCS ensembles :
ID
1
2

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Components

#1: Protein Guanosine deaminase / tRNA-specific adenosine deaminase TAD4 / AtTAD4


Mass: 17098.518 Da / Num. of mol.: 2 / Mutation: E82Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: GSDA, TAD4, At5g28050 / Production host: Escherichia coli (E. coli) / References: UniProt: Q94BU8, guanosine deaminase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-OMG / O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE


Type: RNA linking / Mass: 377.247 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C11H16N5O8P / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 128 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 47.46 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 1.2 M Na-citrate and 0.1 M HEPES (pH 7.5)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Mar 17, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.3→23.69 Å / Num. obs: 14369 / % possible obs: 99.9 % / Redundancy: 9.1 % / Biso Wilson estimate: 22.1 Å2 / CC1/2: 0.954 / Rmerge(I) obs: 0.515 / Net I/σ(I): 5
Reflection shellResolution: 2.3→2.42 Å / Redundancy: 7.5 % / Rmerge(I) obs: 1.937 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 2074 / CC1/2: 0.36 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7DBF

7dbf


Resolution: 2.3→23.69 Å / SU ML: 0.2715 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.8331 / Stereochemistry target values: CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2382 641 4.47 %
Rwork0.2113 13715 -
obs0.2125 14356 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 28.05 Å2
Refinement stepCycle: LAST / Resolution: 2.3→23.69 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2376 0 44 128 2548
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00592463
X-RAY DIFFRACTIONf_angle_d0.88193328
X-RAY DIFFRACTIONf_chiral_restr0.0455372
X-RAY DIFFRACTIONf_plane_restr0.0057429
X-RAY DIFFRACTIONf_dihedral_angle_d8.15341455
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.480.33231320.29052676X-RAY DIFFRACTION100
2.48-2.730.26941210.2662758X-RAY DIFFRACTION99.97
2.73-3.120.26381160.23032717X-RAY DIFFRACTION100
3.12-3.930.2241540.18542731X-RAY DIFFRACTION100
3.93-23.690.19171180.17122833X-RAY DIFFRACTION99.93

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