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- PDB-1fc5: CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1fc5
TitleCRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
ComponentsMOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
KeywordsBIOSYNTHETIC PROTEIN / molybdopterin / four modules / with magnesium / Montreal-Kingston Bacterial Structural Genomics Initiative / BSGI / Structural Genomics
Function / homology
Function and homology information


molybdopterin molybdotransferase / molybdopterin molybdotransferase activity / Mo-molybdopterin cofactor biosynthetic process / protein homodimerization activity / identical protein binding / metal ion binding / cytoplasm / cytosol
Similarity search - Function
Molybdopterin biosynthesis moeA protein; domain 3 / Molybdopterin biosynthesis moea protein, domain 3. / Beta-clip / MoeA, C-terminal, domain IV / Molybdenum cofactor biosynthesis proteins signature 2. / Molybdopterin biosynthesis moea protein, domain 2 / MoeA, N-terminal and linker domain / MoeA, C-terminal, domain IV / MoeA, N-terminal and linker domain superfamily / MoeA, C-terminal, domain IV superfamily ...Molybdopterin biosynthesis moeA protein; domain 3 / Molybdopterin biosynthesis moea protein, domain 3. / Beta-clip / MoeA, C-terminal, domain IV / Molybdenum cofactor biosynthesis proteins signature 2. / Molybdopterin biosynthesis moea protein, domain 2 / MoeA, N-terminal and linker domain / MoeA, C-terminal, domain IV / MoeA, N-terminal and linker domain superfamily / MoeA, C-terminal, domain IV superfamily / Molybdopterin biosynthesis protein MoeA-like / MoeA N-terminal region (domain I and II) / MoeA C-terminal region (domain IV) / Molybdopterin biosynthesis moea protein, domain 2 / Molybdenum cofactor biosynthesis, conserved site / MoaB/Mog-like domain / Molybdenum Cofactor Biosythetic Enzyme; Chain A / MoaB/Mog domain / MoaB/Mog-like domain superfamily / Probable molybdopterin binding domain / Probable molybdopterin binding domain / Beta Complex / Alpha-Beta Complex / Beta Barrel / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Molybdopterin molybdenumtransferase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.2 Å
AuthorsHuang, W. / Cygler, M. / Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
CitationJournal: J.Mol.Biol. / Year: 2001
Title: The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
Authors: Schrag, J.D. / Huang, W. / Sivaraman, J. / Smith, C. / Plamondon, J. / Larocque, R. / Matte, A. / Cygler, M.
History
DepositionJul 17, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 25, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Jan 31, 2018Group: Advisory / Atomic model / Experimental preparation
Category: atom_site / exptl_crystal_grow / pdbx_distant_solvent_atoms
Item: _exptl_crystal_grow.temp

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
B: MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,0114
Polymers88,9622
Non-polymers492
Water9,008500
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5660 Å2
ΔGint-44 kcal/mol
Surface area35020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.640, 101.850, 103.440
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsThe biological assembly is a dimer constructed from chain A a symmetry partner generated by the two-fold.

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Components

#1: Protein MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN


Mass: 44481.215 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P12281
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 500 / 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: 2.27 Å3/Da / Density % sol: 45.76 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.5
Details: PEG8000, Cacodylate, pH 6.5, VAPOR DIFFUSION, temperature 20K
Crystal
*PLUS
Density % sol: 44 %
Crystal grow
*PLUS
pH: 7.5 / Method: vapor diffusion, hanging drop / Details: used macroseeding
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
115 %(w/v)PEG80001reservoir
2100 mM1reservoirMgCl2
3100 mMsodium cacodylate1reservoir
45 mMdithiothreitol1reservoir
51 %(v/v)ethylene glycol1reservoir
610 mg/mlprotein1drop
710 mMTris1drop
85 mMdithiothreitol1drop

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X8C / Wavelength: 0.9795
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: May 28, 2000
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.2→50 Å / Num. all: 41012 / Num. obs: 231130 / % possible obs: 98.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.8 % / Biso Wilson estimate: 40 Å2 / Rmerge(I) obs: 0.059 / Net I/σ(I): 19.6
Reflection shellResolution: 2.2→2.23 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.255 / % possible all: 88.3
Reflection
*PLUS
Lowest resolution: 20 Å / Num. obs: 40862 / Num. measured all: 232716 / Rmerge(I) obs: 0.067
Reflection shell
*PLUS
% possible obs: 88.3 % / Rmerge(I) obs: 0.209 / Mean I/σ(I) obs: 12.6

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Processing

Software
NameClassification
SOLVEphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementResolution: 2.2→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.297 1641 random
Rwork0.253 --
all0.26 40862 -
obs0.26 40862 -
Refinement stepCycle: LAST / Resolution: 2.2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6076 0 2 220 6298
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.44
Software
*PLUS
Name: CNS / Classification: refinement
Refinement
*PLUS
Lowest resolution: 50 Å / σ(F): 0 / Rfactor obs: 0.226 / Rfactor Rfree: 0.277
Solvent computation
*PLUS
Displacement parameters
*PLUS

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