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- PDB-1jwa: Structure of the ATP-bound MoeB-MoaD Protein Complex -

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Basic information

Entry
Database: PDB / ID: 1jwa
TitleStructure of the ATP-bound MoeB-MoaD Protein Complex
Components
  • MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN
  • MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1
KeywordsLIGASE / MoeB: modified Rossmann fold / MoaD: ubiquitin-like fold
Function / homology
Function and homology information


molybdopterin-synthase adenylyltransferase / molybdopterin-synthase adenylyltransferase activity / molybdopterin synthase complex / molybdopterin adenylyltransferase complex / ubiquitin-like modifier activating enzyme activity / sulfotransferase activity / thiosulfate-cyanide sulfurtransferase activity / Mo-molybdopterin cofactor biosynthetic process / nucleotidyltransferase activity / nucleotide binding ... molybdopterin-synthase adenylyltransferase / molybdopterin-synthase adenylyltransferase activity / molybdopterin synthase complex / molybdopterin adenylyltransferase complex / ubiquitin-like modifier activating enzyme activity / sulfotransferase activity / thiosulfate-cyanide sulfurtransferase activity / Mo-molybdopterin cofactor biosynthetic process / nucleotidyltransferase activity / nucleotide binding / protein homodimerization activity / ATP binding / metal ion binding / cytoplasm / cytosol
Similarity search - Function
Molybdopterin synthase sulfurylase MoeB / Molybdopterin synthase sulfur carrier subunit / Sulfur carrier ThiS/MoaD-like / ThiS family / Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp / ThiF/MoeB/HesA family / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / Beta-grasp domain ...Molybdopterin synthase sulfurylase MoeB / Molybdopterin synthase sulfur carrier subunit / Sulfur carrier ThiS/MoaD-like / ThiS family / Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp / ThiF/MoeB/HesA family / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / Beta-grasp domain / Beta-grasp domain superfamily / Ubiquitin-like (UB roll) / NAD(P)-binding Rossmann-like Domain / Roll / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Molybdopterin-synthase adenylyltransferase / Molybdopterin synthase sulfur carrier subunit
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.9 Å
AuthorsLake, M.W. / Wuebbens, M.M. / Rajagopalan, K.V. / Schindelin, H.
CitationJournal: Nature / Year: 2001
Title: Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Authors: Lake, M.W. / Wuebbens, M.M. / Rajagopalan, K.V. / Schindelin, H.
History
DepositionSep 3, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 21, 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
Revision 1.4Feb 7, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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
B: MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN
D: MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,0143
Polymers35,5072
Non-polymers5071
Water00
1
B: MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN
D: MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1
hetero molecules

B: MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN
D: MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,0286
Polymers71,0134
Non-polymers1,0142
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_665-y+1,-x+1,-z+1/21
Buried area10810 Å2
ΔGint-58 kcal/mol
Surface area21950 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)78.723, 78.723, 103.184
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
DetailsThe asymmetric unit contains a heterodimer comprised of (1) molecule of MoeB and (1) molecule of MoaD. The heterotetramer is generated by applying: -y+1,-x+1,1/2-z

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Components

#1: Protein MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN


Mass: 26741.791 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: MoeB / Plasmid: pET15B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P12282
#2: Protein MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1 / MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN D


Mass: 8764.880 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: MoaD / Plasmid: pET15B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P30748
#3: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM

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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: 2.25 Å3/Da / Density % sol: 45.34 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: Lithium Sulfate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Crystal grow
*PLUS
Temperature: 4 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
123 mg/mlMoeB1drop
210 mg/mlMoaD1drop
31.7 M1reservoirLi2SO4
4100 mMHEPES1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1.1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 24, 2000
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.9→50 Å / Num. all: 7355 / Num. obs: 7355 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rmerge(I) obs: 0.143 / Net I/σ(I): 9.4
Reflection shellResolution: 2.9→3.02 Å / Rmerge(I) obs: 0.362 / Mean I/σ(I) obs: 2.4 / % possible all: 100
Reflection
*PLUS

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Processing

Software
NameClassification
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.9→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: REFMAC Dictionary
RfactorNum. reflection% reflectionSelection details
Rfree0.26756 288 4.1 %RANDOM
Rwork0.20302 ---
all0.20569 6696 --
obs0.20569 6696 94.7 %-
Displacement parametersBiso mean: 49.754 Å2
Baniso -1Baniso -2Baniso -3
1--0.24 Å20 Å20 Å2
2---0.24 Å20 Å2
3---0.48 Å2
Refinement stepCycle: LAST / Resolution: 2.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2237 0 31 0 2268
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0190.022
X-RAY DIFFRACTIONp_mcbond_it2.0221.5
X-RAY DIFFRACTIONp_mcangle_it3.5512
X-RAY DIFFRACTIONp_scbond_it5.3413
X-RAY DIFFRACTIONp_scangle_it8.4324.5
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.9 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 4.1 % / Rfactor obs: 0.203
Solvent computation
*PLUS
Displacement parameters
*PLUS

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