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- PDB-6ioi: Crystal structure of Homoserine O-acetyltransferase in complex wi... -

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Basic information

Entry
Database: PDB / ID: 6ioi
TitleCrystal structure of Homoserine O-acetyltransferase in complex with CoA from Mycobacterium smegmatis ATCC 19420
ComponentsHomoserine O-acetyltransferase
KeywordsTRANSFERASE / BIOSYNTHETIC PROTEIN
Function / homology
Function and homology information


homoserine metabolic process / homoserine O-acetyltransferase / homoserine O-acetyltransferase activity / methionine biosynthetic process / cytoplasm
Similarity search - Function
Homoserine/serine acetyltransferase MetX-like / alpha/beta hydrolase fold / Alpha/beta hydrolase fold-1 / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
COENZYME A / Homoserine O-acetyltransferase / Homoserine O-acetyltransferase
Similarity search - Component
Biological speciesMycobacterium smegmatis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsSagong, H.-Y. / Kim, K.-J.
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2019
Title: Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420.
Authors: Sagong, H.Y. / Hong, J. / Kim, K.J.
History
DepositionOct 30, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 4, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Homoserine O-acetyltransferase
B: Homoserine O-acetyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,4874
Polymers78,9522
Non-polymers1,5352
Water10,395577
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6080 Å2
ΔGint-17 kcal/mol
Surface area26250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.384, 96.366, 140.670
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Homoserine O-acetyltransferase / HAT / Homoserine transacetylase / HTA


Mass: 39475.992 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium smegmatis (bacteria) / Gene: metX_1, metXA, ERS451418_01697 / Plasmid: pET30a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21_T1R(DE3)
References: UniProt: A0A0D6HE46, UniProt: A0QSZ0*PLUS, homoserine O-acetyltransferase
#2: Chemical ChemComp-COA / COENZYME A


Mass: 767.534 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 577 / 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: 2.56 Å3/Da / Density % sol: 51.99 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 34 % (v/v) polyethylene glycol (PEG) 400, 0.1 M Sodium acetate/acetic acid pH 5.5, 0.2 M calcium acetate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 0.97934 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 24, 2018
RadiationMonochromator: Double Crystal Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 1.6→50 Å / Num. obs: 105196 / % possible obs: 99.9 % / Redundancy: 7.2 % / Net I/σ(I): 46
Reflection shellResolution: 1.6→1.63 Å / Redundancy: 7.1 % / Mean I/σ(I) obs: 9.56 / Num. unique obs: 5234 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
HKL-2000data reduction
PDB_EXTRACT3.24data extraction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6IOG

6iog


Resolution: 1.6→30.14 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.948 / SU B: 1.39 / SU ML: 0.05 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.084 / ESU R Free: 0.084 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2064 5222 5 %RANDOM
Rwork0.1806 ---
obs0.1819 99881 99.79 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 125.86 Å2 / Biso mean: 16.62 Å2 / Biso min: 8.06 Å2
Baniso -1Baniso -2Baniso -3
1--0.15 Å20 Å20 Å2
2--0.68 Å2-0 Å2
3----0.53 Å2
Refinement stepCycle: final / Resolution: 1.6→30.14 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5482 0 96 577 6155
Biso mean--53.49 25.16 -
Num. residues----740
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0135715
X-RAY DIFFRACTIONr_bond_other_d0.0010.0175207
X-RAY DIFFRACTIONr_angle_refined_deg1.7691.6447817
X-RAY DIFFRACTIONr_angle_other_deg1.5641.57512019
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2255740
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.26520.9300
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.2815815
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.9331550
X-RAY DIFFRACTIONr_chiral_restr0.0940.2733
X-RAY DIFFRACTIONr_gen_planes_refined0.010.026598
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021202
LS refinement shellResolution: 1.6→1.642 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.249 394 -
Rwork0.197 7258 -
all-7652 -
obs--99.53 %

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