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- PDB-5xd3: Crystal structure of Mycobacterium smegmatis MutT1 in complex wit... -

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Basic information

Entry
Database: PDB / ID: 5xd3
TitleCrystal structure of Mycobacterium smegmatis MutT1 in complex with ATP (I)
ComponentsNUDIX family proteinNudix hydrolase
KeywordsHYDROLASE / Nudix enzyme / histidine phosphatase domain / intermolecular interface binding / diadenosine polyphosphates / enzyme action / fluoride inhibition
Function / homology
Function and homology information


8-oxo-(d)GTP phosphatase / diadenosine hexaphosphate hydrolase (ATP-forming) / 8-oxo-dGDP phosphatase / 8-oxo-GDP phosphatase activity / 8-oxo-dGDP phosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / DNA replication / DNA repair / metal ion binding
Similarity search - Function
Phosphoglycerate mutase family / Histidine phosphatase superfamily, clade-1 / Histidine phosphatase superfamily (branch 1) / Histidine phosphatase superfamily / NUDIX hydrolase / NUDIX hydrolase, conserved site / Nudix box signature. / NUDIX domain / Nudix hydrolase domain profile. / NUDIX hydrolase domain / NUDIX hydrolase-like domain superfamily
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / 8-oxo-(d)GTP phosphatase
Similarity search - Component
Biological speciesMycobacterium smegmatis (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.78 Å
AuthorsArif, S.M. / Varshney, U. / Vijayan, M.
Citation
Journal: J. Struct. Biol. / Year: 2017
Title: Hydrolysis of diadenosine polyphosphates. Exploration of an additional role of Mycobacterium smegmatis MutT1
Authors: Arif, S.M. / Varshney, U. / Vijayan, M.
#1: Journal: Acta Crystallogr. D Biol. Crystallogr. / Year: 2017
Title: Biochemical and structural studies of Mycobacterium smegmatis MutT1, a sanitization enzyme with unusual modes of association
Authors: Arif, S.M. / Patil, A.G. / Varshney, U. / Vijayan, M.
#2: Journal: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Year: 2012
Title: Crystallization and preliminary X-ray studies of MutT1 (MSMEG_2390) from Mycobacterium smegmatis.
Authors: Arif, S.M. / Patil, A.G. / Varshney, U. / Vijayan, M.
History
DepositionMar 24, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 9, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
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.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NUDIX family protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,2845
Polymers38,1531
Non-polymers1,1314
Water5,368298
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area920 Å2
ΔGint-10 kcal/mol
Surface area13750 Å2
MethodPISA
Unit cell
Length a, b, c (Å)42.030, 84.210, 43.790
Angle α, β, γ (deg.)90.00, 92.89, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein NUDIX family protein / Nudix hydrolase


Mass: 38153.148 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Strain: ATCC 700084 / mc(2)155 / Gene: MSMEG_2390 / Production host: Escherichia coli (E. coli) / Strain (production host): JW0097 / References: UniProt: A0QUZ2
#2: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 298 / 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: 2.03 Å3/Da / Density % sol: 39.37 %
Crystal growTemperature: 293 K / Method: microbatch / pH: 8.5
Details: 0.2M sodium acetate trihydrate, 0.1M Tris-HCl pH 8.5, 30%(w/v) PEG4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.54179 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Apr 13, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54179 Å / Relative weight: 1
ReflectionResolution: 1.78→38.81 Å / Num. obs: 28450 / % possible obs: 97.3 % / Redundancy: 5 % / Net I/σ(I): 12.9
Reflection shellResolution: 1.78→1.88 Å / Redundancy: 5 % / Mean I/σ(I) obs: 1.8 / Num. unique obs: 4037 / % possible all: 94.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
iMOSFLMdata processing
SCALAdata scaling
PHASERphasing
iMOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5gg5

5gg5


Resolution: 1.78→38.81 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.959 / SU B: 3.227 / SU ML: 0.096 / Cross valid method: THROUGHOUT / ESU R: 0.12 / ESU R Free: 0.118 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20447 1433 5 %RANDOM
Rwork0.16214 ---
obs0.16428 27012 97.38 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 30.899 Å2
Baniso -1Baniso -2Baniso -3
1--1.02 Å20 Å21 Å2
2---0.97 Å2-0 Å2
3---1.88 Å2
Refinement stepCycle: 1 / Resolution: 1.78→38.81 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2292 0 69 298 2659
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.0192439
X-RAY DIFFRACTIONr_bond_other_d0.0010.022309
X-RAY DIFFRACTIONr_angle_refined_deg1.8881.9923331
X-RAY DIFFRACTIONr_angle_other_deg0.86535302
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5625295
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.52422.455110
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.54415397
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.5311528
X-RAY DIFFRACTIONr_chiral_restr0.1050.2361
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0212711
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02555
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.4712.7181177
X-RAY DIFFRACTIONr_mcbond_other2.4672.7141176
X-RAY DIFFRACTIONr_mcangle_it3.5194.0551473
X-RAY DIFFRACTIONr_mcangle_other3.524.0581474
X-RAY DIFFRACTIONr_scbond_it3.6023.2231262
X-RAY DIFFRACTIONr_scbond_other3.5953.2241262
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.4494.6571859
X-RAY DIFFRACTIONr_long_range_B_refined7.63624.2552953
X-RAY DIFFRACTIONr_long_range_B_other7.42923.5032826
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.78→1.826 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.396 95 -
Rwork0.358 1981 -
obs--94.97 %

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