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- PDB-3a8j: Crystal Structure of ET-EHred complex -

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Basic information

Entry
Database: PDB / ID: 3a8j
TitleCrystal Structure of ET-EHred complex
Components
  • Aminomethyltransferase
  • Glycine cleavage system H protein
KeywordsTRANSFERASE/TRANSPORT PROTEIN / Glycine Cleavage System / Aminotransferase / Transferase / Lipoyl / TRANSFERASE-TRANSPORT PROTEIN COMPLEX
Function / homology
Function and homology information


aminomethyltransferase / aminomethyltransferase activity / glycine decarboxylation via glycine cleavage system / glycine cleavage complex / transaminase activity / one-carbon metabolic process / cytoplasm / cytosol
Similarity search - Function
Glycine cleavage system T protein, bacteria / Aminomethyltransferase fragment / Aminomethyltransferase fragment / Glycine cleavage system T protein / Aminomethyltransferase beta-barrel domains / Aminomethyltransferase beta-barrel domains / Glycine cleavage system H-protein, subgroup / Glycine cleavage system H-protein / Glycine cleavage system H-protein/Simiate / Glycine cleavage H-protein ...Glycine cleavage system T protein, bacteria / Aminomethyltransferase fragment / Aminomethyltransferase fragment / Glycine cleavage system T protein / Aminomethyltransferase beta-barrel domains / Aminomethyltransferase beta-barrel domains / Glycine cleavage system H-protein, subgroup / Glycine cleavage system H-protein / Glycine cleavage system H-protein/Simiate / Glycine cleavage H-protein / Glycine cleavage T-protein, C-terminal barrel domain / Glycine cleavage T-protein C-terminal barrel domain / Glycine cleavage T-protein/YgfZ, C-terminal / Probable tRNA modification gtpase trme; domain 1 / Aminomethyltransferase-like / Aminomethyltransferase, folate-binding domain / GCVT N-terminal domain / GTP-binding protein TrmE/Aminomethyltransferase GcvT, domain 1 / 2-oxo acid dehydrogenase, lipoyl-binding site / 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Gyrase A; domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Few Secondary Structures / Irregular / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Alpha-Beta Plaits / Beta Barrel / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Glycine cleavage system H protein / Aminomethyltransferase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.98 Å
AuthorsOkamura-Ikeda, K. / Hosaka, H.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related ...Title: Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism
Authors: Okamura-Ikeda, K. / Hosaka, H. / Maita, N. / Fujiwara, K. / Yoshizawa, A.C. / Nakagawa, A. / Taniguchi, H.
History
DepositionOct 6, 2009Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 7, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 21, 2013Group: Database references
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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aminomethyltransferase
B: Aminomethyltransferase
C: Aminomethyltransferase
D: Aminomethyltransferase
E: Glycine cleavage system H protein
F: Glycine cleavage system H protein


Theoretical massNumber of molelcules
Total (without water)188,7816
Polymers188,7816
Non-polymers00
Water24,5361362
1
A: Aminomethyltransferase
E: Glycine cleavage system H protein


Theoretical massNumber of molelcules
Total (without water)54,2002
Polymers54,2002
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Aminomethyltransferase
F: Glycine cleavage system H protein


Theoretical massNumber of molelcules
Total (without water)54,2002
Polymers54,2002
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Aminomethyltransferase


Theoretical massNumber of molelcules
Total (without water)40,1911
Polymers40,1911
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Aminomethyltransferase


Theoretical massNumber of molelcules
Total (without water)40,1911
Polymers40,1911
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.024, 88.527, 97.237
Angle α, β, γ (deg.)91.51, 102.16, 89.66
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Aminomethyltransferase / Glycine cleavage system T protein


Mass: 40190.602 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 substr. W3110 / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P27248, aminomethyltransferase
#2: Protein Glycine cleavage system H protein


Mass: 14009.418 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 substr. W3110 / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P0A6T9
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1362 / 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: 2.41 Å3/Da / Density % sol: 48.9 %
Crystal growTemperature: 288 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 16% PEG8000, 0.04M KH2PO4, 20% Glycerol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: Bruker DIP-6040 / Detector: CCD / Date: Dec 5, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.98→50 Å / Num. obs: 112820 / % possible obs: 98 % / Redundancy: 2.1 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 15.3
Reflection shellResolution: 2→2.07 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.346 / Mean I/σ(I) obs: 2.4

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Processing

Software
NameVersionClassification
HKL-2000data collection
MOLREPphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3AB9 (EHred), 1VLO (ET)

3ab9

1vlo


Resolution: 1.98→44.42 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.923 / SU B: 4.156 / SU ML: 0.117 / Cross valid method: THROUGHOUT / ESU R: 0.182 / ESU R Free: 0.175 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2383 5960 5 %RANDOM
Rwork0.17245 ---
obs0.1757 112820 97.17 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 27.822 Å2
Baniso -1Baniso -2Baniso -3
1--0.44 Å2-0.16 Å2-1.21 Å2
2---0.56 Å2-0.1 Å2
3---0.48 Å2
Refinement stepCycle: LAST / Resolution: 1.98→44.42 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13198 0 0 1362 14560
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0220.02213528
X-RAY DIFFRACTIONr_angle_refined_deg1.7991.95418358
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.77751717
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.33824.231631
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.574152216
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.2041590
X-RAY DIFFRACTIONr_chiral_restr0.1270.22037
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.02110392
X-RAY DIFFRACTIONr_mcbond_it1.0771.58481
X-RAY DIFFRACTIONr_mcangle_it1.817213595
X-RAY DIFFRACTIONr_scbond_it3.00535047
X-RAY DIFFRACTIONr_scangle_it4.6694.54758
LS refinement shellResolution: 1.982→2.033 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.305 413 -
Rwork0.236 7327 -
obs--86.36 %

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