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- PDB-7wq0: Methionyl-tRNA synthetase from Staphylococcus aureus complexed wi... -

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Basic information

Entry
Database: PDB / ID: 7wq0
TitleMethionyl-tRNA synthetase from Staphylococcus aureus complexed with a fragment and ATP
ComponentsMethionine--tRNA ligase
KeywordsLIGASE/INHIBITOR / LIGASE-INHIBITOR COMPLEX
Function / homology
Function and homology information


methionine-tRNA ligase / methionine-tRNA ligase activity / methionyl-tRNA aminoacylation / tRNA binding / ATP binding / cytoplasm
Similarity search - Function
Methionyl-tRNA synthetase, beta subunit, C-terminal / Methionine-tRNA synthetase, type 2 / Methionyl-tRNA synthetase / Methioninyl-tRNA synthetase core domain / Methionyl-tRNA synthetase, anticodon-binding domain / Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding / Anticodon-binding domain of tRNA ligase / tRNA-binding domain / Putative tRNA binding domain / tRNA-binding domain profile. ...Methionyl-tRNA synthetase, beta subunit, C-terminal / Methionine-tRNA synthetase, type 2 / Methionyl-tRNA synthetase / Methioninyl-tRNA synthetase core domain / Methionyl-tRNA synthetase, anticodon-binding domain / Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding / Anticodon-binding domain of tRNA ligase / tRNA-binding domain / Putative tRNA binding domain / tRNA-binding domain profile. / Methionyl/Leucyl tRNA synthetase / tRNA synthetases class I (M) / Aminoacyl-tRNA synthetase, class Ia, anticodon-binding / Aminoacyl-tRNA synthetase, class I, conserved site / Aminoacyl-transfer RNA synthetases class-I signature. / Rossmann-like alpha/beta/alpha sandwich fold / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / TRANS-2-PHENYLCYCLOPROPYLAMINE / Methionine--tRNA ligase
Similarity search - Component
Biological speciesStaphylococcus aureus subsp. aureus COL (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.09 Å
AuthorsYi, J. / Cai, Z. / Qiu, H. / Lu, F. / Chen, B. / Luo, Z. / Gu, Q. / Xu, J. / Zhou, H.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)22177140 China
National Natural Science Foundation of China (NSFC)81773636 China
CitationJournal: Nucleic Acids Res. / Year: 2022
Title: Fragment screening and structural analyses highlight the ATP-assisted ligand binding for inhibitor discovery against type 1 methionyl-tRNA synthetase.
Authors: Yi, J. / Cai, Z. / Qiu, H. / Lu, F. / Luo, Z. / Chen, B. / Gu, Q. / Xu, J. / Zhou, H.
History
DepositionJan 24, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 27, 2022Provider: repository / Type: Initial release
Revision 1.1May 18, 2022Group: Database references / Category: citation
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 23, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Nov 29, 2023Group: 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: Methionine--tRNA ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,0568
Polymers61,1041
Non-polymers9527
Water1,53185
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area810 Å2
ΔGint-3 kcal/mol
Surface area21090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.276, 72.716, 118.710
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 Methionine--tRNA ligase / Methionyl-tRNA synthetase / MetRS


Mass: 61103.969 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus subsp. aureus COL (bacteria)
Strain: COL / Gene: metG / Production host: Escherichia coli (E. coli) / References: UniProt: Q5HII6, methionine-tRNA ligase
#2: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
#3: Chemical ChemComp-TPA / TRANS-2-PHENYLCYCLOPROPYLAMINE


Mass: 134.198 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H12N / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 85 / 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: 2.09 Å3/Da / Density % sol: 41.25 %
Crystal growTemperature: 300 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: Sodium cacodylate, PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.97914 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Dec 1, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97914 Å / Relative weight: 1
ReflectionResolution: 2.09→46.02 Å / Num. obs: 30973 / % possible obs: 99.7 % / Redundancy: 6.5 % / CC1/2: 0.991 / Rmerge(I) obs: 0.153 / Rpim(I) all: 0.065 / Rrim(I) all: 0.167 / Net I/σ(I): 9.4
Reflection shellResolution: 2.09→2.15 Å / Redundancy: 6 % / Rmerge(I) obs: 0.508 / Num. unique obs: 2306 / CC1/2: 0.872 / Rpim(I) all: 0.225 / Rrim(I) all: 0.557 / % possible all: 97

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Processing

Software
NameVersionClassification
REFMAC5.8.0232refinement
Aimless0.7.3data scaling
PDB_EXTRACT3.27data extraction
XDSdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7WPK

7wpk


Resolution: 2.09→46.02 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.891 / SU B: 5.5 / SU ML: 0.147 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.272 / ESU R Free: 0.204 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2494 1544 5 %RANDOM
Rwork0.2126 ---
obs0.2145 29369 99.58 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 57.66 Å2 / Biso mean: 19.778 Å2 / Biso min: 5.76 Å2
Baniso -1Baniso -2Baniso -3
1-2.08 Å20 Å20 Å2
2---0.21 Å20 Å2
3----1.87 Å2
Refinement stepCycle: final / Resolution: 2.09→46.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4182 0 61 85 4328
Biso mean--30.84 22.47 -
Num. residues----518
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0020.0134357
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173916
X-RAY DIFFRACTIONr_angle_refined_deg1.1831.6455920
X-RAY DIFFRACTIONr_angle_other_deg1.1421.5779102
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9575519
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.86223.436227
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.5715718
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.4281518
X-RAY DIFFRACTIONr_chiral_restr0.0490.2557
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.024908
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02910
LS refinement shellResolution: 2.092→2.146 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.295 86 -
Rwork0.254 2098 -
all-2184 -
obs--96.85 %

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