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- PDB-7q2g: mycolic acid methyltransferase Hma (MmaA4) from Mycobac-terium tu... -

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Basic information

Entry
Database: PDB / ID: 7q2g
Titlemycolic acid methyltransferase Hma (MmaA4) from Mycobac-terium tuberculosis in complex with ZT726
ComponentsHydroxymycolate synthase MmaA4
KeywordsTRANSFERASE / mycolic acid methyltransferase mycobacterium tuberculosis fragment based ligand discovery
Function / homology
Function and homology information


mycolic acid biosynthetic process / S-adenosylmethionine-dependent methyltransferase activity / peptidoglycan-based cell wall / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / methylation / plasma membrane
Similarity search - Function
: / Mycolic acid cyclopropane synthase / : / Mycolic acid cyclopropane synthetase / S-adenosyl-L-methionine-dependent methyltransferase superfamily
Similarity search - Domain/homology
8-oxidanylquinoline-2-carbaldehyde / Hydroxymycolate synthase MmaA4
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2 Å
AuthorsMaveyraud, L. / Galy, R. / Mourey, L.
Funding support France, 2items
OrganizationGrant numberCountry
Centre National de la Recherche Scientifique (CNRS) France
Universite de Toulouse France
CitationJournal: Pharmaceuticals / Year: 2021
Title: Fragment-Based Ligand Discovery Applied to the Mycolic Acid Methyltransferase Hma (MmaA4) from Mycobacterium tuberculosis : A Crystallographic and Molecular Modelling Study.
Authors: Galy, R. / Ballereau, S. / Genisson, Y. / Mourey, L. / Plaquevent, J.C. / Maveyraud, L.
History
DepositionOct 25, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 2, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Hydroxymycolate synthase MmaA4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,8796
Polymers36,5211
Non-polymers3585
Water99155
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)57.060, 57.060, 205.930
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

#1: Protein Hydroxymycolate synthase MmaA4 / Mycolic acid methyltransferase / MA-MT / S-adenosylmethionine-dependent methyltransferase / AdoMet-MT / SAM-MT


Mass: 36521.305 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: mmaA4, hma, mma4, Rv0642c / Plasmid: pET25b / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q79FX8, Transferases; Transferring one-carbon groups; Methyltransferases
#2: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-8MJ / 8-oxidanylquinoline-2-carbaldehyde


Mass: 173.168 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H7NO2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 55 / 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: 2.65 Å3/Da / Density % sol: 53.58 %
Crystal growTemperature: 285 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: BisTris 50 mM, PEG 3350 4% (w/v), pH 6.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 3, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9393 Å / Relative weight: 1
ReflectionResolution: 2→40.1 Å / Num. obs: 27352 / % possible obs: 99.9 % / Redundancy: 7.46 % / CC1/2: 0.996 / Rrim(I) all: 0.099 / Rsym value: 0.091 / Net I/σ(I): 11.39
Reflection shellResolution: 2→2.12 Å / Redundancy: 7.6 % / Num. unique obs: 4359 / CC1/2: 0.814 / Rrim(I) all: 1.437 / Rsym value: 1.339 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
XDSdata reduction
XDSdata scaling
XSCALEdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 2fk7

2fk7


Resolution: 2→40.14 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.937 / SU B: 13.202 / SU ML: 0.164 / Cross valid method: THROUGHOUT / ESU R: 0.18 / ESU R Free: 0.179 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25382 1191 5.2 %RANDOM
Rwork0.19261 ---
obs0.19562 21807 84.07 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 71.508 Å2
Baniso -1Baniso -2Baniso -3
1-0.83 Å20.42 Å20 Å2
2--0.83 Å2-0 Å2
3----2.7 Å2
Refinement stepCycle: 1 / Resolution: 2→40.14 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2264 0 20 55 2339
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0132337
X-RAY DIFFRACTIONr_bond_other_d0.0090.0172136
X-RAY DIFFRACTIONr_angle_refined_deg1.2261.6483163
X-RAY DIFFRACTIONr_angle_other_deg1.231.5814925
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3375280
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.56122.045132
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.115391
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3211516
X-RAY DIFFRACTIONr_chiral_restr0.0510.2295
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.022714
X-RAY DIFFRACTIONr_gen_planes_other0.0070.02558
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_it9.85924.0881124
X-RAY DIFFRACTIONr_mcbond_other9.8624.1071125
X-RAY DIFFRACTIONr_mcangle_it9.8834.7161403
X-RAY DIFFRACTIONr_mcangle_other9.89634.7241403
X-RAY DIFFRACTIONr_scbond_it11.5226.981213
X-RAY DIFFRACTIONr_scbond_other11.51626.9871214
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other12.99137.9711761
X-RAY DIFFRACTIONr_long_range_B_refined12.64774.52555
X-RAY DIFFRACTIONr_long_range_B_other12.6474.4542543
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.051 Å
RfactorNum. reflection% reflection
Rfree0.368 110 -
Rwork0.349 1863 -
obs--99.5 %
Refinement TLS params.Method: refined / Origin x: 25.7099 Å / Origin y: 7.9958 Å / Origin z: 16.6208 Å
111213212223313233
T0.1156 Å20.0122 Å2-0.0074 Å2-0.0515 Å2-0.0009 Å2--0.0205 Å2
L1.2244 °2-0.1638 °2-0.5824 °2-2.3317 °2-0.1033 °2--2.9083 °2
S-0.0796 Å °0.0601 Å °0.1434 Å °-0.0756 Å °0.188 Å °-0.055 Å °-0.3933 Å °-0.154 Å °-0.1084 Å °

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