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- PDB-3usq: Structure of D159S/Y194F glycogenin mutant truncated at residue 270 -

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Basic information

Entry
Database: PDB / ID: 3usq
TitleStructure of D159S/Y194F glycogenin mutant truncated at residue 270
ComponentsGlycogenin-1
KeywordsTRANSFERASE / Glucosyltransferase
Function / homology
Function and homology information


glycogenin glucosyltransferase / glycogenin glucosyltransferase activity / glycogen biosynthetic process / manganese ion binding / protein homodimerization activity / nucleus / cytoplasm
Similarity search - Function
: / Glycosyl transferase, family 8 / Glycosyl transferase family 8 / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Nucleotide-diphospho-sugar transferases / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Biological speciesOryctolagus cuniculus (rabbit)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.4 Å
AuthorsIssoglio, F.M. / Carrizo, M.E. / Romero, J.M. / Curtino, J.A.
CitationJournal: J.Biol.Chem. / Year: 2012
Title: Mechanisms of monomeric and dimeric glycogenin autoglucosylation.
Authors: Issoglio, F.M. / Carrizo, M.E. / Romero, J.M. / Curtino, J.A.
History
DepositionNov 23, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 14, 2011Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2012Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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

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Assembly

Deposited unit
A: Glycogenin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7834
Polymers32,5641
Non-polymers2203
Water1,17165
1
A: Glycogenin-1
hetero molecules

A: Glycogenin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,5678
Polymers65,1272
Non-polymers4396
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_545-x,-y-1,z1
Buried area3220 Å2
ΔGint-21 kcal/mol
Surface area21000 Å2
MethodPISA
2
A: Glycogenin-1
hetero molecules

A: Glycogenin-1
hetero molecules

A: Glycogenin-1
hetero molecules

A: Glycogenin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,13316
Polymers130,2554
Non-polymers87912
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_545-x,-y-1,z1
crystal symmetry operation3_556-x,y,-z+11
crystal symmetry operation4_546x,-y-1,-z+11
Buried area10140 Å2
ΔGint-196 kcal/mol
Surface area38800 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.530, 105.640, 120.080
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222
Components on special symmetry positions
IDModelComponents
11A-319-

HOH

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Components

#1: Protein Glycogenin-1 / GN-1 / GN1


Mass: 32563.658 Da / Num. of mol.: 1 / Mutation: D159S,Y194F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: GYG, GYG1 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta(DE3) / References: UniProt: P13280, glycogenin glucosyltransferase
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 65 / 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: 2.75 Å3/Da / Density % sol: 55.32 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 12% PEGMME5000/0.2M ammonium sulfate/sodium MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: LNLS / Beamline: D03B-MX1 / Wavelength: 1.43 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Apr 14, 2010 / Details: mirrors
RadiationMonochromator: Silicium curved crystal, with asymmetric 7.25 angle cut
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.43 Å / Relative weight: 1
ReflectionResolution: 2.4→79.32 Å / Num. all: 14436 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 1.9
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.397 / Mean I/σ(I) obs: 1.9 / Num. unique all: 2075 / % possible all: 100

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.4→79.32 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.902 / SU B: 7.442 / SU ML: 0.177 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.328 / ESU R Free: 0.248 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25919 726 5 %RANDOM
Rwork0.21276 ---
obs0.21512 13710 99.81 %-
all-13710 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 35.901 Å2
Baniso -1Baniso -2Baniso -3
1-2.29 Å20 Å20 Å2
2---0.31 Å20 Å2
3----1.99 Å2
Refinement stepCycle: LAST / Resolution: 2.4→79.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2029 0 13 65 2107
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0222091
X-RAY DIFFRACTIONr_angle_refined_deg1.3071.9432845
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8995254
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.64124.23992
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.43815334
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.927158
X-RAY DIFFRACTIONr_chiral_restr0.0850.2326
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0211563
X-RAY DIFFRACTIONr_mcbond_it0.781.51276
X-RAY DIFFRACTIONr_mcangle_it1.45722071
X-RAY DIFFRACTIONr_scbond_it1.713815
X-RAY DIFFRACTIONr_scangle_it2.844.5774
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.301 58 -
Rwork0.275 998 -
obs--100 %

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