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- PDB-1ya6: alpha-glucosyltransferase in complex with UDP and a 13-mer DNA co... -

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Basic information

Entry
Database: PDB / ID: 1ya6
Titlealpha-glucosyltransferase in complex with UDP and a 13-mer DNA containing a central A:G mismatch
Components
  • 5'-D(*AP*TP*AP*CP*TP*AP*AP*GP*AP*TP*AP*G)-3'
  • 5'-D(*CP*TP*AP*TP*CP*TP*GP*AP*GP*TP*AP*T)-3'
  • DNA alpha-glucosyltransferase
KeywordsTRANSFERASE/DNA / glycosyltransferase/DNA / TRANSFERASE-DNA complex
Function / homology
Function and homology information


DNA alpha-glucosyltransferase / DNA alpha-glucosyltransferase activity / symbiont-mediated suppression of host adaptive immune response / symbiont-mediated suppression of host CRISPR-cas system / symbiont-mediated evasion of host restriction-modification system / DNA modification / symbiont-mediated suppression of host innate immune response
Similarity search - Function
DNA alpha-glucosyltransferase / DNA alpha-glucosyltransferase / Glycogen Phosphorylase B; / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
COBALT HEXAMMINE(III) / URIDINE-5'-DIPHOSPHATE / DNA / DNA (> 10) / DNA alpha-glucosyltransferase
Similarity search - Component
Biological speciesEnterobacteria phage T4 (virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsLariviere, L. / Sommer, N. / Morera, S.
CitationJournal: J.Mol.Biol. / Year: 2005
Title: Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase.
Authors: Lariviere, L. / Sommer, N. / Morera, S.
History
DepositionDec 17, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Aug 30, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 25, 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_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

Downloads & links

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Assembly

Deposited unit
C: 5'-D(*AP*TP*AP*CP*TP*AP*AP*GP*AP*TP*AP*G)-3'
D: 5'-D(*CP*TP*AP*TP*CP*TP*GP*AP*GP*TP*AP*T)-3'
A: DNA alpha-glucosyltransferase
B: DNA alpha-glucosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,36613
Polymers101,4304
Non-polymers1,9369
Water3,261181
1
C: 5'-D(*AP*TP*AP*CP*TP*AP*AP*GP*AP*TP*AP*G)-3'
A: DNA alpha-glucosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,6236
Polymers50,7362
Non-polymers8884
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: 5'-D(*CP*TP*AP*TP*CP*TP*GP*AP*GP*TP*AP*T)-3'
B: DNA alpha-glucosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,7427
Polymers50,6942
Non-polymers1,0495
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)45.855, 119.318, 86.812
Angle α, β, γ (deg.)90.00, 92.87, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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DNA chain , 2 types, 2 molecules CD

#1: DNA chain 5'-D(*AP*TP*AP*CP*TP*AP*AP*GP*AP*TP*AP*G)-3'


Mass: 3694.455 Da / Num. of mol.: 1 / Source method: obtained synthetically
#2: DNA chain 5'-D(*CP*TP*AP*TP*CP*TP*GP*AP*GP*TP*AP*T)-3'


Mass: 3652.402 Da / Num. of mol.: 1 / Source method: obtained synthetically

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Protein , 1 types, 2 molecules AB

#3: Protein DNA alpha-glucosyltransferase / AGT


Mass: 47041.379 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Plasmid: proexhtb / Production host: Escherichia coli (E. coli) / Strain (production host): xl1blue / References: UniProt: P04519, DNA alpha-glucosyltransferase

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Non-polymers , 3 types, 190 molecules

#4: Chemical
ChemComp-NCO / COBALT HEXAMMINE(III)


Mass: 161.116 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: CoH18N6
#5: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 181 / 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: 2.5 Å3/Da / Density % sol: 49.8 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Components of the solutions
IDNameCrystal-IDSol-ID
1H2O11
2H2O12

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Sep 25, 2004
RadiationMonochromator: 0.97 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 2.4→20 Å / Num. all: 36383 / Num. obs: 36229 / % possible obs: 99.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 7 % / Biso Wilson estimate: 58 Å2 / Rsym value: 0.073 / Net I/σ(I): 8.8
Reflection shellResolution: 2.4→2.49 Å / % possible all: 99.6

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNS1refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1Y8Z

1y8z


Resolution: 2.4→20 Å / σ(F): 1 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.28 1795 random
Rwork0.23 --
all-36383 -
obs-36229 -
Refinement stepCycle: LAST / Resolution: 2.4→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6209 488 99 182 6978
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_angle_deg1.268

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