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- PDB-4a9a: Structure of Rbg1 in complex with Tma46 dfrp domain -

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Basic information

Entry
Database: PDB / ID: 4a9a
TitleStructure of Rbg1 in complex with Tma46 dfrp domain
Components
  • RIBOSOME-INTERACTING GTPASE 1
  • TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46
KeywordsTRANSLATION / DRG-DFRP COMPLEX / RIBOSOME BINDING GTPASE
Function / homology
Function and homology information


: / positive regulation of cellular response to amino acid starvation / cytoplasmic stress granule / cytoplasmic translation / mRNA binding / GTP binding / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Helix Hairpins - #1070 / MYOD Basic-Helix-Loop-Helix Domain, subunit B - #10 / MYOD Basic-Helix-Loop-Helix Domain, subunit B / ZC3H15/TMA46 family, C-terminal / DRG Family Regulatory Proteins, Tma46 / GTP binding protein, second domain / C-terminal region of MMR_HSR1 domain / GTP1/OBG, conserved site / GTP1/OBG family signature. / TGS domain ...Helix Hairpins - #1070 / MYOD Basic-Helix-Loop-Helix Domain, subunit B - #10 / MYOD Basic-Helix-Loop-Helix Domain, subunit B / ZC3H15/TMA46 family, C-terminal / DRG Family Regulatory Proteins, Tma46 / GTP binding protein, second domain / C-terminal region of MMR_HSR1 domain / GTP1/OBG, conserved site / GTP1/OBG family signature. / TGS domain / Zinc finger, CCCH-type superfamily / zinc finger / TGS domain profile. / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / TGS / TGS-like / OBG-type guanine nucleotide-binding (G) domain / OBG-type guanine nucleotide-binding (G) domain profile. / Beta-grasp domain / 50S ribosome-binding GTPase / Other non-globular / GTP binding domain / Helix Hairpins / Beta-grasp domain superfamily / Helix non-globular / Special / Ubiquitin-like (UB roll) / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Roll / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Ribosome-interacting GTPase 1 / Translation machinery-associated protein 46
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.67 Å
AuthorsFrancis, S.M. / Gas, M. / Daugeron, M. / Seraphin, B. / Bravo, J.
CitationJournal: Nucleic Acids Res. / Year: 2012
Title: Rbg1-Tma46 Dimer Structure Reveals New Functional Domains and Their Role in Polysome Recruitment.
Authors: Francis, S.M. / Gas, M. / Daugeron, M. / Bravo, J. / Seraphin, B.
History
DepositionNov 25, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 3, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 19, 2012Group: Database references
Revision 1.2Jan 25, 2017Group: Data collection
Revision 1.3May 8, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RIBOSOME-INTERACTING GTPASE 1
B: RIBOSOME-INTERACTING GTPASE 1
C: TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46
D: TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46


Theoretical massNumber of molelcules
Total (without water)115,5124
Polymers115,5124
Non-polymers00
Water1,38777
1
A: RIBOSOME-INTERACTING GTPASE 1
C: TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46


Theoretical massNumber of molelcules
Total (without water)57,7562
Polymers57,7562
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5900 Å2
ΔGint-42.5 kcal/mol
Surface area24530 Å2
MethodPISA
2
B: RIBOSOME-INTERACTING GTPASE 1
D: TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46


Theoretical massNumber of molelcules
Total (without water)57,7562
Polymers57,7562
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4570 Å2
ΔGint-34.1 kcal/mol
Surface area23790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)86.200, 224.890, 84.890
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein RIBOSOME-INTERACTING GTPASE 1 / GTP-BINDING PROTEIN RBG1 / GENETICALLY INTERACTS WITH RIBOSOMAL GENES PROTEIN 1 / RBG1


Mass: 41717.035 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Plasmid: PBS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIPL / References: UniProt: P39729
#2: Protein TRANSLATION MACHINERY-ASSOCIATED PROTEIN 46 / DRG FAMILY-REGULATORY PROTEIN 1 / TMA46


Mass: 16039.022 Da / Num. of mol.: 2 / Fragment: DFRP DOMAIN, RESIDUES 205-345
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Plasmid: PBS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIPL / References: UniProt: Q12000
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 77 / 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: 2

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Sample preparation

CrystalDensity Matthews: 3.55 Å3/Da / Density % sol: 65.41 % / Description: NONE
Crystal growpH: 7
Details: 2.38 SODIUM FORMATE, 0.2-0.25 SODIUM CITRATE PH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9795
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 5, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.67→79.42 Å / Num. obs: 47671 / % possible obs: 99.9 % / Observed criterion σ(I): 1.9 / Redundancy: 7.14 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.5
Reflection shellResolution: 2.67→2.82 Å / Redundancy: 7 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 1.9 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.6.0117refinement
MOSFLMdata reduction
SCALAdata scaling
SHARPphasing
RefinementMethod to determine structure: SIRAS
Starting model: NONE

Resolution: 2.67→56.22 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.948 / SU B: 18.68 / SU ML: 0.181 / Cross valid method: THROUGHOUT / ESU R: 0.331 / ESU R Free: 0.234 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.22212 1200 2.5 %RANDOM
Rwork0.1959 ---
obs0.19655 46457 99.96 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 76.935 Å2
Baniso -1Baniso -2Baniso -3
1--0.39 Å20 Å20 Å2
2--0.15 Å20 Å2
3---0.24 Å2
Refinement stepCycle: LAST / Resolution: 2.67→56.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7030 0 0 77 7107
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0197132
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2331.9839613
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.6485893
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.64224.637289
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.555151367
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.1931543
X-RAY DIFFRACTIONr_chiral_restr0.0850.21128
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0215145
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.672→2.741 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.349 92 -
Rwork0.35 3140 -
obs--99.91 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.43340.0287-0.75475.41651.289420.39220.1269-0.0308-0.87510.2576-0.5051-0.32051.17340.74070.37820.4191-0.0262-0.19850.5623-0.03480.287971.057617.039471.5766
22.65961.7799-0.43972.5903-0.33571.93840.0723-0.1282-0.0620.1876-0.0467-0.211-0.0380.2761-0.02560.07030.0089-0.03330.1103-0.03710.077554.780816.002647.4237
312.9989-3.73936.2559.10151.514412.3432-0.5121-1.00111.24150.6659-0.03570.2786-1.4867-0.17420.54780.6844-0.0854-0.0840.4513-0.19050.284364.348834.167573.0216
49.64330.2457-2.173312.8158-0.945.02230.29930.32540.3208-1.267-0.1593-0.7876-0.39940.1248-0.140.38510.0140.1470.092-0.04620.435955.518344.341733.9234
510.64158.98614.977411.25735.51859.39820.7364-0.73851.6491.5675-0.80731.6539-0.321-0.25830.07090.4494-0.09030.30740.4356-0.08330.379435.646511.634762.3998
65.62941.4642-1.181428.9172-0.0735.6312-0.0360.04931.05840.76190.19251.1165-1.0111-0.0341-0.15660.22880.05160.00340.1682-0.03670.312631.610721.18845.9349
71.29234.2219-0.211115.51732.654813.65190.0780.0980.9325-0.49770.08992.83610.0724-2.1258-0.16790.5415-0.0735-0.08110.5332-0.02161.246139.082743.501434.9632
82.69091.71311.956151.6725-3.16451.8849-0.1194-0.32580.2249-2.45720.20810.5396-0.1774-0.4358-0.08871.6360.47670.82460.54920.18210.867159.098440.320822.0759
911.19055.0717-0.188217.626-6.51594.0506-0.41620.62260.0369-1.93380.1189-0.59520.55710.02150.29730.3278-0.0029-0.00680.2138-0.01270.08350.613318.1529.1142
102.49121.26212.77927.3272-0.031121.1623-0.0269-0.0335-0.34160.2398-0.0390.33830.4875-1.11160.06590.2869-0.0628-0.14820.55590.02120.26271.697123.767210.6398
1111.31421.85783.358710.4619-0.791110.2838-0.77361.1511.2781-0.32850.0443-0.2818-1.75740.29710.72930.719-0.1429-0.20450.47640.17670.341380.058439.80549.2382
123.4354-1.20460.22742.4989-0.18091.98650.09410.2886-0.2604-0.1771-0.04020.10890.12610.0037-0.05380.1411-0.0525-0.08650.1546-0.0350.197589.198918.615132.3649
137.1871-1.5611-0.714221.34143.22443.87560.2007-0.41240.60170.2159-0.26850.7241-0.3482-0.32840.06780.302-0.0354-0.02190.1235-0.09570.510287.939244.598247.5347
148.3654-6.91641.26696.9963-4.980412.49410.69211.01291.0082-0.8104-0.9294-0.96490.52650.41860.23740.59170.14980.16941.0251-0.18260.5611107.911712.001617.9984
159.06223.52640.029724.11056.01218.5323-0.0501-0.02411.378-2.4499-0.29130.4009-1.22620.21840.34140.3425-0.0602-0.10350.36980.05720.4749111.990320.044635.5057
1613.2671-11.09110.233830.5874.456215.9116-0.14940.45380.80221.58612.1404-4.66850.68142.0809-1.9910.5199-0.0805-0.30820.858-0.61321.9843104.109242.504951.1755
1729.3956-5.072313.529323.74037.116210.1661-0.9584-0.3782-0.1671.61950.76010.3840.11610.15150.19820.31220.0169-0.11640.2240.16310.30896.11317.127848.7571
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 45
2X-RAY DIFFRACTION2A53 - 125
3X-RAY DIFFRACTION2A131 - 174
4X-RAY DIFFRACTION2A233 - 299
5X-RAY DIFFRACTION3A175 - 232
6X-RAY DIFFRACTION4A300 - 369
7X-RAY DIFFRACTION5C214 - 240
8X-RAY DIFFRACTION6C241 - 267
9X-RAY DIFFRACTION7C268 - 282
10X-RAY DIFFRACTION8C302 - 313
11X-RAY DIFFRACTION9C314 - 339
12X-RAY DIFFRACTION10B2 - 53
13X-RAY DIFFRACTION11B175 - 232
14X-RAY DIFFRACTION12B54 - 91
15X-RAY DIFFRACTION12B98 - 125
16X-RAY DIFFRACTION12B133 - 174
17X-RAY DIFFRACTION12B233 - 299
18X-RAY DIFFRACTION13B300 - 369
19X-RAY DIFFRACTION14D214 - 240
20X-RAY DIFFRACTION15D241 - 267
21X-RAY DIFFRACTION16D268 - 282
22X-RAY DIFFRACTION17D320 - 339

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