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- PDB-3aen: Reaction intermediate structure of Entamoeba histolytica methioni... -

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Basic information

Entry
Database: PDB / ID: 3aen
TitleReaction intermediate structure of Entamoeba histolytica methionine gamma-lyase 1 containing Michaelis complex and alpha-amino-alpha, beta-butenoic acid-pyridoxal-5'-phosphate
Components(Methionine gamma- ...) x 2
KeywordsLYASE / gamma-lyase / L-methionine / entamoeba histolytica
Function / homology
Function and homology information


methionine gamma-lyase / methionine gamma-lyase activity / transsulfuration / pyridoxal phosphate binding / cytoplasm
Similarity search - Function
Cys/Met metabolism, pyridoxal phosphate-dependent enzyme / Cys/Met metabolism PLP-dependent enzyme / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex ...Cys/Met metabolism, pyridoxal phosphate-dependent enzyme / Cys/Met metabolism PLP-dependent enzyme / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-4LM / METHIONINE / Methionine gamma-lyase
Similarity search - Component
Biological speciesEntamoeba histolytica (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsKaraki, T. / Sato, D. / Shimizu, A. / Nozaki, T. / Harada, S.
CitationJournal: To be Published
Title: Crystal structure of Entamoeba histolytica methionine gamma-lyase 1
Authors: Karaki, T. / Sato, D. / Shimizu, A. / Nozaki, T. / Harada, S.
History
DepositionFeb 10, 2010Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 9, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 11, 2017Group: Refinement description / Category: software
Revision 1.3Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Methionine gamma-lyase
B: Methionine gamma-lyase
C: Methionine gamma-lyase
D: Methionine gamma-lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,33414
Polymers169,8594
Non-polymers1,47410
Water15,745874
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19930 Å2
ΔGint-132 kcal/mol
Surface area47620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.156, 85.428, 114.746
Angle α, β, γ (deg.)90.000, 101.900, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Methionine gamma- ... , 2 types, 4 molecules ACBD

#1: Protein Methionine gamma-lyase


Mass: 42578.902 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Entamoeba histolytica (eukaryote) / Gene: metg / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: Q86D28, methionine gamma-lyase
#2: Protein Methionine gamma-lyase


Mass: 42350.785 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Entamoeba histolytica (eukaryote) / Gene: metg / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: Q86D28, methionine gamma-lyase

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Non-polymers , 5 types, 884 molecules

#3: Chemical ChemComp-MET / METHIONINE


Type: L-peptide linking / Mass: 149.211 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H11NO2S
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-4LM / (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid


Mass: 330.230 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H15N2O7P
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 874 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence details1. ACCORDING TO AUTHOR, THE SUBSTITUTION OF LEU TO SER AT A308, B808, C1308, D1808 ARE ALLELIC ...1. ACCORDING TO AUTHOR, THE SUBSTITUTION OF LEU TO SER AT A308, B808, C1308, D1808 ARE ALLELIC VARIATION. 2. SINCE THE GENE HAD INTERNAL METHIONINE AND UPSTREAM OF THIS MET IS SIMILAR TO SHINE-DALGARNO SEQUENCE, SEVERAL NUCLEOTIDES WERE REPLACED NOT TO CHANGE THE AMINO ACID RESIDUES, BUT AVOID RIBOSOME BINDING IN E. COLI EXPRESSION SYSTEM.

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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: 2.8 Å3/Da / Density % sol: 56.06 % / Mosaicity: 0.431 °
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.6
Details: 1.8M (NH4)2SO4, 0.1M cacodylate buffer, 0.1M Li3(C3H5O(COO)3), 0.1mM pyridozxal 5'-phosphate, pH 6.6, vapor diffusion, sitting drop, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: May 20, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 123826 / % possible obs: 99.4 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.087 / Χ2: 0.887 / Net I/σ(I): 14.13
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.368 / Mean I/σ(I) obs: 2.621 / Num. unique all: 10473 / Χ2: 0.736 / % possible all: 95.8

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.15 Å46.92 Å
Translation2.15 Å46.92 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3ACZ

3acz


Resolution: 2→46.92 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.948 / WRfactor Rfree: 0.18 / WRfactor Rwork: 0.152 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.887 / SU B: 7.46 / SU ML: 0.092 / SU R Cruickshank DPI: 0.149 / SU Rfree: 0.134 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.149 / ESU R Free: 0.134 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.198 6219 5 %RANDOM
Rwork0.166 ---
obs0.168 117579 97.73 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 92.27 Å2 / Biso mean: 32.039 Å2 / Biso min: 10.7 Å2
Baniso -1Baniso -2Baniso -3
1-0.15 Å20 Å20.02 Å2
2--0.13 Å20 Å2
3----0.26 Å2
Refinement stepCycle: LAST / Resolution: 2→46.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11782 0 90 874 12746
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02212130
X-RAY DIFFRACTIONr_angle_refined_deg1.4831.9716414
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.69451548
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.56524.624465
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.824152103
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.0341536
X-RAY DIFFRACTIONr_chiral_restr0.1110.21865
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0218926
X-RAY DIFFRACTIONr_mcbond_it0.6711.57683
X-RAY DIFFRACTIONr_mcangle_it1.224212370
X-RAY DIFFRACTIONr_scbond_it2.20934447
X-RAY DIFFRACTIONr_scangle_it3.4574.54040
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.288 416 -
Rwork0.275 7324 -
all-7740 -
obs-7740 82.99 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.8272-0.24570.26340.39630.0331.9418-0.02310.1944-0.2258-0.06260.01030.06370.208-0.26270.01280.1203-0.0601-0.0290.1281-0.0540.19550.89-14.07534.995
21.6621-0.0569-0.14150.4820.15650.45020.00350.10550.121-0.0211-0.01830.1285-0.0262-0.04490.01480.0962-0.0033-0.02610.05750.01960.2223-12.883.95445.917
31.11220.0235-0.10421.50110.54380.74760.02-0.00650.19310.0048-0.04720.0952-0.0246-0.10220.02720.10030.0127-0.02340.0808-0.00220.24541.96718.10257.28
40.46440.1445-0.09740.3558-0.55451.9972-0.03530.2599-0.2635-0.16610.0342-0.07160.27130.00360.00110.187-0.0239-0.00440.1655-0.11350.226717.715-17.87428.435
51.2945-0.17170.04040.6742-0.08931.10450.05490.5345-0.0123-0.227-0.0362-0.16350.04540.134-0.01870.12670.00740.06470.268-0.04230.099435.831-4.12613.112
61.3758-0.7468-1.23821.82080.25922.25360.23280.26990.5077-0.3675-0.0244-0.3601-0.40960.2496-0.20840.2787-0.06780.11130.40010.18550.284931.90716.2410.224
70.7952-0.3833-0.87970.46540.24662.39580.08590.08460.2505-0.0862-0.0027-0.107-0.2630.3126-0.08320.143-0.06220.00220.15570.05970.240524.76615.08734.447
81.5082-0.09080.09390.4642-0.18520.4242-0.00640.0814-0.0598-0.028-0.0335-0.10980.04610.02730.040.1038-0.0058-0.00930.0578-0.0140.223937.96-3.19745.267
91.19550.08340.20131.4332-0.40630.71360.02870.0002-0.18370.0076-0.0184-0.05780.01480.0981-0.01020.10620.0078-0.0130.0883-0.0020.238123.967-18.37557.388
100.7972-0.3667-0.29460.47940.29631.76330.03390.26260.2591-0.1327-0.02360.0268-0.1991-0.0617-0.01030.1558-0.015-0.02280.13730.09660.21638.31318.16329.795
111.74090.0432-0.38530.72380.19971.0856-0.02220.64770.2099-0.21020.06940.1906-0.1072-0.2707-0.04720.1168-0.0029-0.09510.32680.13070.1484-12.5927.85617.625
122.31330.18780.21421.43570.26731.592-0.08620.7601-0.2508-0.39040.10170.15040.1653-0.3914-0.01550.215-0.1169-0.07390.5822-0.10710.0907-4.481-10.8926.884
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 66
2X-RAY DIFFRACTION2A67 - 251
3X-RAY DIFFRACTION3A252 - 390
4X-RAY DIFFRACTION4B503 - 566
5X-RAY DIFFRACTION5B567 - 811
6X-RAY DIFFRACTION6B812 - 888
7X-RAY DIFFRACTION7C1003 - 1055
8X-RAY DIFFRACTION8C1056 - 1252
9X-RAY DIFFRACTION9C1253 - 1389
10X-RAY DIFFRACTION10D1505 - 1562
11X-RAY DIFFRACTION11D1563 - 1745
12X-RAY DIFFRACTION12D1746 - 1888

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