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- PDB-1iq8: Crystal Structure of archaeosine tRNA-guanine transglycosylase fr... -

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Basic information

Entry
Database: PDB / ID: 1iq8
TitleCrystal Structure of archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii
ComponentsARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE
KeywordsTRANSFERASE / (ALPHA/BETA)8 BARREL / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics
Function / homology
Function and homology information


tRNA-guanine15 transglycosylase / pentosyltransferase activity / tRNA modification / RNA binding / metal ion binding
Similarity search - Function
Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 2 / ArcTGT, C1 domain / tRNA-guanine(15) transglycosylase / tRNA-guanine transglycosylase, patch-forming domain C2 / tRNA-guanine(15) transglycosylase, C1 domain / ArcTGT, C1 domain superfamily / C1 domain of tRNA-guanine transglycosylase dimerisation / Patch-forming domain C2 of tRNA-guanine transglycosylase / ArcTGT, C2 domain / TGT, patch-forming C2 domain superfamily ...Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 2 / ArcTGT, C1 domain / tRNA-guanine(15) transglycosylase / tRNA-guanine transglycosylase, patch-forming domain C2 / tRNA-guanine(15) transglycosylase, C1 domain / ArcTGT, C1 domain superfamily / C1 domain of tRNA-guanine transglycosylase dimerisation / Patch-forming domain C2 of tRNA-guanine transglycosylase / ArcTGT, C2 domain / TGT, patch-forming C2 domain superfamily / Uncharacterised domain CHP00451 / PUA domain / PUA domain / Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 4 / Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase / PUA domain / PUA domain profile. / PUA domain superfamily / Queuine tRNA-ribosyltransferase-like / tRNA-guanine(15) transglycosylase-like / Queuine tRNA-ribosyltransferase-like / Queuine tRNA-ribosyltransferase / PUA-like superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / TIM Barrel / Roll / Alpha-Beta Barrel / Alpha-Beta Complex / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
tRNA-guanine(15) transglycosylase
Similarity search - Component
Biological speciesPyrococcus horikoshii (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.2 Å
AuthorsIshitani, R. / Nureki, O. / Fukai, S. / Kijimoto, T. / Nameki, N. / Watanabe, M. / Kondo, H. / Sekine, M. / Okada, N. / Nishimura, S. ...Ishitani, R. / Nureki, O. / Fukai, S. / Kijimoto, T. / Nameki, N. / Watanabe, M. / Kondo, H. / Sekine, M. / Okada, N. / Nishimura, S. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: J.Mol.Biol. / Year: 2002
Title: Crystal structure of archaeosine tRNA-guanine transglycosylase.
Authors: Ishitani, R. / Nureki, O. / Fukai, S. / Kijimoto, T. / Nameki, N. / Watanabe, M. / Kondo, H. / Sekine, M. / Okada, N. / Nishimura, S. / Yokoyama, S.
History
DepositionJul 9, 2001Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 22, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 31, 2018Group: Experimental preparation / Category: exptl_crystal_grow
Item: _exptl_crystal_grow.pdbx_details / _exptl_crystal_grow.temp
Revision 1.4Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _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
A: ARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE
B: ARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,5806
Polymers133,4002
Non-polymers1794
Water5,242291
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4330 Å2
ΔGint-20 kcal/mol
Surface area42430 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.282, 99.282, 363.740
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein ARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE


Mass: 66700.141 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Plasmid: pET3A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: O58843, tRNA-guanosine34 preQ1 transglycosylase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-MG / MAGNESIUM ION


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


Mass: 18.015 Da / Num. of mol.: 291 / 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: 3.36 Å3/Da / Density % sol: 63.37 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: sodium phosphate, potassium phosphate, sodium acetate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystal grow
*PLUS
Details: Ishitani, R., (2001) Acta Cryst., D57, 1659.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: OXFORD PX210 / Detector: CCD / Date: Nov 20, 2000 / Details: mirrors
RadiationMonochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.2→50 Å / Num. all: 530165 / Num. obs: 530165 / % possible obs: 95.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6 % / Biso Wilson estimate: 19.7 Å2 / Rmerge(I) obs: 0.092 / Rsym value: 0.092 / Net I/σ(I): 34
Reflection shellResolution: 2.2→2.24 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 7.1 / Num. unique all: 4241 / Rsym value: 0.256 / % possible all: 93
Reflection
*PLUS
Lowest resolution: 50 Å / Num. obs: 88967 / Num. measured all: 530165 / Rmerge(I) obs: 0.092
Reflection shell
*PLUS
% possible obs: 93 % / Num. unique obs: 4241 / Num. measured obs: 17411 / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 7.1

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Processing

Software
NameVersionClassification
SHARPphasing
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MAD / Resolution: 2.2→50 Å / Isotropic thermal model: Overall / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.261 9102 9.99 %RANDOM
Rwork0.227 ---
obs-91138 --
Displacement parametersBiso mean: 40.4 Å2
Baniso -1Baniso -2Baniso -3
1-4.43 Å20 Å20 Å2
2--4.43 Å20 Å2
3----8.87 Å2
Refinement stepCycle: LAST / Resolution: 2.2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9304 0 4 291 9599
Refinement
*PLUS
Lowest resolution: 50 Å / Rfactor obs: 0.227 / Rfactor Rfree: 0.261 / Rfactor Rwork: 0.227
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.00634
X-RAY DIFFRACTIONo_angle_d
X-RAY DIFFRACTIONo_angle_deg1.28
X-RAY DIFFRACTIONo_improper_angle_d
X-RAY DIFFRACTIONo_improper_angle_deg0.857

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