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- PDB-1jik: Crystal structure of S. aureus TyrRS in complex with SB-243545 -

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Basic information

Entry
Database: PDB / ID: 1jik
TitleCrystal structure of S. aureus TyrRS in complex with SB-243545
Componentstyrosyl-tRNA synthetase
KeywordsLIGASE / tyrosyl-trna synthetase / staphylococcus aureus / truncation / structure based inhibitor design
Function / homology
Function and homology information


tyrosyl-tRNA aminoacylation / tyrosine-tRNA ligase / tyrosine-tRNA ligase activity / RNA binding / ATP binding / cytoplasm
Similarity search - Function
Tyrosine-tRNA ligase, bacterial-type, type 1 / Tyrosine-tRNA ligase, bacterial-type / Tyrosine-tRNA ligase / Tyrosyl-Transfer RNA Synthetase / Tyrosyl-Transfer RNA Synthetase / Aminoacyl-tRNA synthetase, class Ic / tRNA synthetases class I (W and Y) / Aminoacyl-tRNA synthetase, class I, conserved site / Aminoacyl-transfer RNA synthetases class-I signature. / HUPs ...Tyrosine-tRNA ligase, bacterial-type, type 1 / Tyrosine-tRNA ligase, bacterial-type / Tyrosine-tRNA ligase / Tyrosyl-Transfer RNA Synthetase / Tyrosyl-Transfer RNA Synthetase / Aminoacyl-tRNA synthetase, class Ic / tRNA synthetases class I (W and Y) / Aminoacyl-tRNA synthetase, class I, conserved site / Aminoacyl-transfer RNA synthetases class-I signature. / HUPs / Rossmann-like alpha/beta/alpha sandwich fold / S4 RNA-binding domain / RNA-binding S4 domain / RNA-binding S4 domain superfamily / S4 domain / S4 RNA-binding domain profile. / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-545 / : / Tyrosine--tRNA ligase
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsQiu, X. / Janson, C.A. / Smith, W.W. / Jarvest, R.L.
CitationJournal: Protein Sci. / Year: 2001
Title: Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.
Authors: Qiu, X. / Janson, C.A. / Smith, W.W. / Green, S.M. / McDevitt, P. / Johanson, K. / Carter, P. / Hibbs, M. / Lewis, C. / Chalker, A. / Fosberry, A. / Lalonde, J. / Berge, J. / Brown, P. / ...Authors: Qiu, X. / Janson, C.A. / Smith, W.W. / Green, S.M. / McDevitt, P. / Johanson, K. / Carter, P. / Hibbs, M. / Lewis, C. / Chalker, A. / Fosberry, A. / Lalonde, J. / Berge, J. / Brown, P. / Houge-Frydrych, C.S. / Jarvest, R.L.
History
DepositionJul 2, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 26, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 2.0Feb 7, 2024Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _atom_site.occupancy / _database_2.pdbx_DOI ..._atom_site.occupancy / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: tyrosyl-tRNA synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,1272
Polymers47,6551
Non-polymers4721
Water43224
1
A: tyrosyl-tRNA synthetase
hetero molecules

A: tyrosyl-tRNA synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,2544
Polymers95,3112
Non-polymers9432
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_655-x+1,-y+1/2,z1
2
A: tyrosyl-tRNA synthetase
hetero molecules

A: tyrosyl-tRNA synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,2544
Polymers95,3112
Non-polymers9432
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_556-x+1/2,y,-z+11
Buried area5060 Å2
ΔGint-32 kcal/mol
Surface area27140 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)66.620, 105.380, 140.580
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Cell settingorthorhombic
Space group name H-MI212121
Components on special symmetry positions
IDModelComponents
11A-501-

HOH

Detailsthe biological assembly is a dimer generated from the monomer in ASU and the operation -x,1/2-y,z

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Components

#1: Protein tyrosyl-tRNA synthetase / E.C.6.1.1.1 / TYROSINE--TRNA LIGASE / TYRRS / Tyrosyl-Transfer RNA Synthetase


Mass: 47655.449 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Variant: aureus N315 / Production host: Escherichia coli (E. coli)
References: GenBank: 13701524, UniProt: A6QHR2*PLUS, tyrosine-tRNA ligase
#2: Chemical ChemComp-545 / [2-AMINO-3-(4-HYDROXY-PHENYL)-PROPIONYLAMINO]-(1,3,4,5-TETRAHYDROXY-4-HYDROXYMETHYL-PIPERIDIN-2-YL)- ACETIC ACID BUTYL ESTER / SB-243545


Mass: 471.501 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H33N3O9
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 24 / 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: 2.59 Å3/Da / Density % sol: 52.48 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.25
Details: PEG 1000, CaCl2, pH 7.25, VAPOR DIFFUSION, SITTING DROP at 298K
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlprotein1drop
212-15 MPEG10001reservoir
30.15 M1reservoirCaCl2
40.2 Mimidazole1reservoir

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: SIEMENS / Detector: AREA DETECTOR / Date: Jun 6, 1997
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.8→20 Å / Num. obs: 9301 / % possible obs: 83 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 2 % / Rmerge(I) obs: 0.101 / Net I/σ(I): 7
Reflection shellResolution: 2.8→2.85 Å / Redundancy: 2 % / Rmerge(I) obs: 0.281 / Mean I/σ(I) obs: 1.9 / % possible all: 77
Reflection
*PLUS
Lowest resolution: 20 Å / % possible obs: 83 % / Num. measured all: 18549
Reflection shell
*PLUS
% possible obs: 77 %

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-GENdata reduction
XDSdata scaling
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→8 Å / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.305 450 5 %random
Rwork0.205 ---
obs-8893 --
Refinement stepCycle: LAST / Resolution: 2.8→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2556 0 33 24 2613
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.014
X-RAY DIFFRACTIONx_angle_deg2.1
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.205
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Type: x_angle_deg / Dev ideal: 2.1

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