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- PDB-1ucx: Crystal structure of proglycinin C12G mutant -

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Basic information

Entry
Database: PDB / ID: 1ucx
TitleCrystal structure of proglycinin C12G mutant
ComponentsGlycinin G1
KeywordsPLANT PROTEIN / proglycinin / soybean / trimer / mutant
Function / homology
Function and homology information


protein storage vacuole / nutrient reservoir activity / endoplasmic reticulum
Similarity search - Function
11-S seed storage protein, conserved site / 11-S plant seed storage proteins signature. / 11-S seed storage protein, plant / : / Cupin / Cupin 1 / Cupin / RmlC-like cupin domain superfamily / Jelly Rolls / RmlC-like jelly roll fold ...11-S seed storage protein, conserved site / 11-S plant seed storage proteins signature. / 11-S seed storage protein, plant / : / Cupin / Cupin 1 / Cupin / RmlC-like cupin domain superfamily / Jelly Rolls / RmlC-like jelly roll fold / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesGlycine max (soybean)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsUtsumi, S. / Adachi, M.
CitationJournal: J.Agric.Food Chem. / Year: 2003
Title: Crystal Structures and Structural Stabilities of the Disulfide Bond-Deficient Soybean Proglycinin Mutants C12G and C88S.
Authors: Adachi, M. / Okuda, E. / Kaneda, Y. / Hashimoto, A. / Shutov, A.D. / Becker, C. / Utsumi, S.
History
DepositionApr 24, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 3, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 10, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Revision 1.5Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glycinin G1
B: Glycinin G1
C: Glycinin G1


Theoretical massNumber of molelcules
Total (without water)160,9093
Polymers160,9093
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15010 Å2
ΔGint-99 kcal/mol
Surface area37780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)115.201, 115.201, 147.420
Angle α, β, γ (deg.)90, 90, 90
Int Tables number76
Space group name H-MP41
DetailsThe asymmetric unit contains a biological unit of a trimer.

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Components

#1: Protein Glycinin G1 / proglycinin


Mass: 53636.406 Da / Num. of mol.: 3 / Mutation: C12G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Glycine max (soybean) / Plasmid: pKK233-2 / Production host: Escherichia coli (E. coli) / Strain (production host): JM105 / References: UniProt: P04776
Has protein modificationY

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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: 4.04 Å3/Da / Density % sol: 69.33 %
Crystal growTemperature: 281 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: PEG6000, sodium cloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 281K
Crystal grow
*PLUS
Temperature: 5 ℃ / pH: 7.6 / Method: vapor diffusion, hanging drop
Details: Gidamis, A.B., (1994) Biosci., Biotechnol., Biochem., 58, 703.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
110 mg/mlprotein1drop
235 mMpotassium phosphate1droppH7.6
30.15 M1dropNaCl
41.5 mMPMSF1drop
51 mMEDTA1drop
610 mM2ME1drop
70.02 %(w/v)1dropNaN3
83-12 %(w/v)PEG60001reservoir

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: ROTATING ANODE / Type: MACSCIENCE / Wavelength: 1.5418 Å
DetectorType: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Sep 18, 1998
RadiationMonochromator: Ni FiLTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 3.2→31.4 Å / Num. all: 108107 / Num. obs: 105297 / % possible obs: 97.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rsym value: 0.141 / Net I/σ(I): 8.75
Reflection shellResolution: 3.2→3.3 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 2.46 / Rsym value: 0.523 / % possible all: 95.6
Reflection
*PLUS
Num. obs: 30085 / Rmerge(I) obs: 0.141
Reflection shell
*PLUS
% possible obs: 95.6 % / Rmerge(I) obs: 0.523

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Processing

Software
NameClassification
SADIEdata collection
SAINTdata reduction
X-PLORmodel building
X-PLORrefinement
SADIEdata reduction
SAINTdata scaling
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.2→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.257 2314 RANDOM
Rwork0.18 --
all0.218 23305 -
obs0.218 23305 -
Refinement stepCycle: LAST / Resolution: 3.2→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8643 0 0 0 8643
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.012
X-RAY DIFFRACTIONx_angle_d3
Refinement
*PLUS
Lowest resolution: 8 Å / % reflection Rfree: 10 % / Rfactor Rwork: 0.18
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_deg3
LS refinement shell
*PLUS
Highest resolution: 3.2 Å / Lowest resolution: 3.3 Å / Rfactor Rfree: 0.311 / Rfactor Rwork: 0.212

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