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- PDB-8sy0: X-ray crystal structure of UDP- 2,3-diacetamido-2,3-dideoxy-glucu... -

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Basic information

Entry
Database: PDB / ID: 8sy0
TitleX-ray crystal structure of UDP- 2,3-diacetamido-2,3-dideoxy-glucuronic acid-2-epimerase from Thermus thermophilus strain HB27 in complex with its product UDP-2,3-diacetamido-2,3-dideoxy-d-mannuronic acid at pH 9
ComponentsUDP-2,3-diacetamido-2,3-dideoxy-glucuronic acid-2-epimerase
KeywordsISOMERASE / lipopolysaccharide / O-antigen / 2-epimerase
Function / homology
Function and homology information


UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) / UDP-N-acetylglucosamine 2-epimerase activity / nucleotide binding
Similarity search - Function
UDP-N-acetylglucosamine 2-epimerase WecB-like / UDP-N-acetylglucosamine 2-epimerase domain / UDP-N-acetylglucosamine 2-epimerase / Glycogen Phosphorylase B; / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-MJ3 / UDP-N-acetylglucosamine 2-epimerase
Similarity search - Component
Biological speciesThermus thermophilus HB27 (bacteria)
MethodX-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.1 Å
AuthorsMcKnight, J.O. / Thoden, J.B. / Holden, H.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM134643 United States
CitationJournal: J.Biol.Chem. / Year: 2023
Title: Structural analysis of a bacterial UDP-sugar 2-epimerase reveals the active site architecture before and after catalysis.
Authors: Thoden, J.B. / McKnight, J.O. / Kroft, C.W. / Jast, J.D.T. / Holden, H.M.
History
DepositionMay 24, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 13, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Database references / Category: citation / Item: _citation.journal_volume

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UDP-2,3-diacetamido-2,3-dideoxy-glucuronic acid-2-epimerase
B: UDP-2,3-diacetamido-2,3-dideoxy-glucuronic acid-2-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,4588
Polymers83,9902
Non-polymers1,4686
Water5,134285
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3330 Å2
ΔGint-34 kcal/mol
Surface area26530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.340, 128.608, 58.934
Angle α, β, γ (deg.)90.00, 111.24, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein UDP-2,3-diacetamido-2,3-dideoxy-glucuronic acid-2-epimerase


Mass: 41995.070 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus HB27 (bacteria) / Strain: ATCC BAA-163 / DSM 7039 / HB27 / Gene: TT_C0285 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2 / References: UniProt: Q72KY0

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Non-polymers , 5 types, 291 molecules

#2: Chemical ChemComp-MJ3 / (2~{S},3~{S},4~{R},5~{S},6~{R})-4,5-diacetamido-6-[[[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3-oxidanyl-oxane-2-carboxylic acid / UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid


Mass: 662.389 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H28N4O18P2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 285 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.37 Å3/Da / Density % sol: 48.09 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9
Details: protein incubated with 5 mM UDP-2,3-diacetamido-2,3-dideoxy-glucuronic acid 18-22% poly(ethylene glycol) 3350, 200 mM LiCl, 100 mM CHES (pH 9)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SEALED TUBE / Type: BRUKER D8 QUEST / Wavelength: 1.5418 Å
DetectorType: Bruker PHOTON II / Detector: PIXEL / Date: Jan 27, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. obs: 45153 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.9 % / Rsym value: 0.082 / Net I/σ(I): 14.7
Reflection shellResolution: 2.1→2.2 Å / Redundancy: 3.5 % / Num. unique obs: 5715 / R split: 2.7 / Rsym value: 0.36 / % possible all: 96.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0403refinement
SAINTdata reduction
SADABSdata scaling
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.1→40.67 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.913 / SU B: 6.328 / SU ML: 0.157 / Cross valid method: THROUGHOUT / ESU R: 0.221 / ESU R Free: 0.186 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23067 2215 4.9 %RANDOM
Rwork0.18038 ---
obs0.18286 42938 99.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 25.943 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å2-0 Å2-0.01 Å2
2--0.02 Å20 Å2
3---0.02 Å2
Refinement stepCycle: 1 / Resolution: 2.1→40.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5676 0 93 285 6054
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0125910
X-RAY DIFFRACTIONr_bond_other_d0.0010.0165705
X-RAY DIFFRACTIONr_angle_refined_deg1.6241.6748031
X-RAY DIFFRACTIONr_angle_other_deg0.5471.58413097
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6875727
X-RAY DIFFRACTIONr_dihedral_angle_2_deg9.348553
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.616101009
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0760.2912
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.026940
X-RAY DIFFRACTIONr_gen_planes_other0.0020.021340
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_it2.3922.4782890
X-RAY DIFFRACTIONr_mcbond_other2.3892.4782890
X-RAY DIFFRACTIONr_mcangle_it3.6294.443611
X-RAY DIFFRACTIONr_mcangle_other3.634.4423612
X-RAY DIFFRACTIONr_scbond_it3.3262.9083020
X-RAY DIFFRACTIONr_scbond_other3.3252.9083021
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.3255.1374417
X-RAY DIFFRACTIONr_long_range_B_refined6.87125.296692
X-RAY DIFFRACTIONr_long_range_B_other6.8725.296693
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.307 154 -
Rwork0.317 3056 -
obs--96.17 %

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