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- PDB-3duf: Snapshots of catalysis in the E1 subunit of the pyruvate dehydrog... -

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Basic information

Entry
Database: PDB / ID: 3duf
TitleSnapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Components
  • (Pyruvate dehydrogenase E1 component subunit ...) x 2
  • Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
KeywordsOXIDOREDUCTASE/TRANSFERASE / OXIDOREDUCTASE / PYRUVATE / DEHYDROGENASE / DIHYDROLIPOYL / ACETYL TRANSFERASE / MULTIENZYME COMPLEX / TRANSFERASE / Glycolysis / Phosphoprotein / Thiamine pyrophosphate / Acyltransferase / OXIDOREDUCTASE-TRANSFERASE COMPLEX
Function / homology
Function and homology information


pyruvate dehydrogenase (acetyl-transferring) / pyruvate dehydrogenase (acetyl-transferring) activity / dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / lipoic acid binding / branched-chain amino acid catabolic process / cytoplasm
Similarity search - Function
Pyruvate dehydrogenase E1 component subunit alpha/BCKADH E1-alpha / : / : / Transketolase, C-terminal domain / Dehydrogenase, E1 component / Dehydrogenase E1 component / Peripheral subunit-binding domain / e3 binding domain / Peripheral subunit-binding (PSBD) domain profile. / E3-binding domain superfamily ...Pyruvate dehydrogenase E1 component subunit alpha/BCKADH E1-alpha / : / : / Transketolase, C-terminal domain / Dehydrogenase, E1 component / Dehydrogenase E1 component / Peripheral subunit-binding domain / e3 binding domain / Peripheral subunit-binding (PSBD) domain profile. / E3-binding domain superfamily / Transketolase, C-terminal domain / Rossmann fold - #920 / 2-oxo acid dehydrogenase, lipoyl-binding site / 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. / 2-oxoacid dehydrogenase acyltransferase, catalytic domain / 2-oxoacid dehydrogenases acyltransferase (catalytic domain) / Transketolase-like, pyrimidine-binding domain / Transketolase, pyrimidine binding domain / Transketolase, pyrimidine binding domain / Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II / Biotin-requiring enzyme / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Chloramphenicol acetyltransferase-like domain superfamily / Thiamin diphosphate-binding fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / Chem-R1T / Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex / Pyruvate dehydrogenase E1 component subunit alpha / Pyruvate dehydrogenase E1 component subunit beta
Similarity search - Component
Biological speciesBacillus stearothermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsPei, X.Y. / Titman, C.M. / Frank, R.A.W. / Leeper, F.J. / Luisi, B.F.
CitationJournal: Structure / Year: 2008
Title: Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multienzyme complex
Authors: Pei, X.Y. / Titman, C.M. / Frank, R.A. / Leeper, F.J. / Luisi, B.F.
History
DepositionJul 17, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 6, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 30, 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 ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pyruvate dehydrogenase E1 component subunit alpha
B: Pyruvate dehydrogenase E1 component subunit beta
C: Pyruvate dehydrogenase E1 component subunit alpha
D: Pyruvate dehydrogenase E1 component subunit beta
I: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
E: Pyruvate dehydrogenase E1 component subunit alpha
F: Pyruvate dehydrogenase E1 component subunit beta
G: Pyruvate dehydrogenase E1 component subunit alpha
H: Pyruvate dehydrogenase E1 component subunit beta
J: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
hetero molecules


Theoretical massNumber of molelcules
Total (without water)402,90921
Polymers400,84010
Non-polymers2,06911
Water7,332407
1
A: Pyruvate dehydrogenase E1 component subunit alpha
B: Pyruvate dehydrogenase E1 component subunit beta
C: Pyruvate dehydrogenase E1 component subunit alpha
D: Pyruvate dehydrogenase E1 component subunit beta
I: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
hetero molecules


Theoretical massNumber of molelcules
Total (without water)201,50612
Polymers200,4205
Non-polymers1,0867
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22300 Å2
ΔGint-137.9 kcal/mol
Surface area43490 Å2
2
E: Pyruvate dehydrogenase E1 component subunit alpha
F: Pyruvate dehydrogenase E1 component subunit beta
G: Pyruvate dehydrogenase E1 component subunit alpha
H: Pyruvate dehydrogenase E1 component subunit beta
J: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
hetero molecules


Theoretical massNumber of molelcules
Total (without water)201,4039
Polymers200,4205
Non-polymers9834
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21810 Å2
ΔGint-131.6 kcal/mol
Surface area44100 Å2
Unit cell
Length a, b, c (Å)69.247, 231.995, 92.614
Angle α, β, γ (deg.)90.00, 90.74, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
12B
22D
32F
42H
13I
23J

NCS domain segments:

Component-ID: 1 / Refine code: 6

Dom-IDEns-IDBeg label comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRLYSAA4 - 3685 - 369
21THRLYSCC4 - 3685 - 369
31THRLYSEF4 - 3685 - 369
41THRLYSGH4 - 3685 - 369
12ALAPHEBB1 - 3242 - 325
22ALAPHEDD1 - 3242 - 325
32ALAPHEFG1 - 3242 - 325
42ALAPHEHI1 - 3242 - 325
13VALALAIE129 - 165129 - 407
23ALAALAJJ130 - 165123 - 165

NCS ensembles :
ID
1
2
3

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Components

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Pyruvate dehydrogenase E1 component subunit ... , 2 types, 8 molecules ACEGBDFH

#1: Protein
Pyruvate dehydrogenase E1 component subunit alpha


Mass: 41518.176 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: pdhA / Plasmid: pKBstE1a / Production host: Escherichia coli (E. coli) / Strain (production host): TG1 recO
References: UniProt: P21873, pyruvate dehydrogenase (acetyl-transferring)
#2: Protein
Pyruvate dehydrogenase E1 component subunit beta


Mass: 35495.633 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: pdhB / Plasmid: pKBstE1b / Production host: Escherichia coli (E. coli) / Strain (production host): TG1 recO
References: UniProt: P21874, pyruvate dehydrogenase (acetyl-transferring)

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Protein , 1 types, 2 molecules IJ

#3: Protein Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex / E2 / Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex


Mass: 46392.215 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: pdhC / Plasmid: pKBstE1a / Production host: Escherichia coli (E. coli) / Strain (production host): TG1 recO
References: UniProt: P11961, dihydrolipoyllysine-residue acetyltransferase

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Non-polymers , 4 types, 418 molecules

#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-R1T / 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1R)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL TRIHYDROGEN DIPHOSPHATE / 2-[(1R)-1-HYDROXYETHYL]-3-DEAZA-THDP


Mass: 467.371 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H23N3O8P2S
#6: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 407 / 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: 1.86 Å3/Da / Density % sol: 33.72 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: The protein solution was then mixed in 1:1 volume ratio of crystallization buffer consisting of 8-12 % mono-methyl ether polyethylene glycol (MME PEG) 5000, 0.1 M Na maleate pH 5.5, and the ...Details: The protein solution was then mixed in 1:1 volume ratio of crystallization buffer consisting of 8-12 % mono-methyl ether polyethylene glycol (MME PEG) 5000, 0.1 M Na maleate pH 5.5, and the droplet was left to equilibrate against a reservoir of neat crystallization buffer., VAPOR DIFFUSION, SITTING DROP, temperature 291.15K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9795 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 11, 2005 / Details: mirror
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.5→66 Å / Num. all: 99540 / Num. obs: 99351 / % possible obs: 98.9 % / Observed criterion σ(F): 2.6 / Observed criterion σ(I): 2.6 / Redundancy: 3.7 % / Rmerge(I) obs: 0.111 / Rsym value: 0.111 / Net I/σ(I): 3.1
Reflection shellResolution: 2.5→2.64 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 5.4 / Rsym value: 0.302 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MxCuBEdata collection
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1W85

1w85


Resolution: 2.5→59.44 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.888 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / ESU R: 1.087 / ESU R Free: 0.328 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26303 5027 5.1 %RANDOM
Rwork0.18848 ---
obs0.19233 94324 98.86 %-
all-94324 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 42.879 Å2
Baniso -1Baniso -2Baniso -3
1-2.23 Å20 Å20.06 Å2
2---0.31 Å20 Å2
3----1.91 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.342 Å1.251 Å
Luzzati d res low-2.5 Å
Luzzati sigma a0.128 Å0.309 Å
Refinement stepCycle: LAST / Resolution: 2.5→59.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21953 0 123 407 22483
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02222510
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2821.97330493
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg1.16152820
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.5624.481038
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.013153820
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.14715148
X-RAY DIFFRACTIONr_chiral_restr0.1330.23368
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0217205
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2440.210110
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3270.215835
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1460.2664
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2590.266
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1250.26
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.9541.514061
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it5.28222608
X-RAY DIFFRACTIONr_scbond_it8.41838449
X-RAY DIFFRACTIONr_scangle_it10.4924.57885
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A2725loose positional0.675
12C2725loose positional0.635
13E2725loose positional0.735
14G2725loose positional0.675
21B2480loose positional0.395
22D2480loose positional0.385
23F2480loose positional0.415
24H2480loose positional0.45
31I203loose positional0.795
11A2725loose thermal2.3410
12C2725loose thermal2.910
13E2725loose thermal3.1810
14G2725loose thermal2.410
21B2480loose thermal2.7410
22D2480loose thermal4.710
23F2480loose thermal3.7510
24H2480loose thermal3.2310
31I203loose thermal0.4910
LS refinement shellResolution: 2.5→2.565 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.296 362 -
Rwork0.222 7060 -
obs--99.88 %

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