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- PDB-4zgq: Structure of Cdc123 bound to eIF2-gammaDIII domain -

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Basic information

Entry
Database: PDB / ID: 4zgq
TitleStructure of Cdc123 bound to eIF2-gammaDIII domain
Components
  • Cell division cycle protein 123
  • Eukaryotic translation initiation factor 2 subunit gamma
KeywordsCELL CYCLE / ATP-grasp fold / eIF2
Function / homology
Function and homology information


eukaryotic translation initiation factor 2 complex assembly / Cellular response to mitochondrial stress / Recycling of eIF2:GDP / ABC-family proteins mediated transport / methionyl-initiator methionine tRNA binding / eukaryotic translation initiation factor 2 complex / multi-eIF complex / selenocysteine metabolic process / eukaryotic 43S preinitiation complex / protein-synthesizing GTPase ...eukaryotic translation initiation factor 2 complex assembly / Cellular response to mitochondrial stress / Recycling of eIF2:GDP / ABC-family proteins mediated transport / methionyl-initiator methionine tRNA binding / eukaryotic translation initiation factor 2 complex / multi-eIF complex / selenocysteine metabolic process / eukaryotic 43S preinitiation complex / protein-synthesizing GTPase / selenocysteine insertion sequence binding / formation of translation preinitiation complex / eukaryotic 48S preinitiation complex / positive regulation of translational fidelity / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / L13a-mediated translational silencing of Ceruloplasmin expression / protein folding chaperone / translation initiation factor binding / translational initiation / translation initiation factor activity / ribosome / GTPase activity / GTP binding / magnesium ion binding / ATP binding / cytoplasm / cytosol
Similarity search - Function
Cell division cycle protein 123 / D123 / Initiation factor eIF2 gamma, domain 2 / Initiation factor eIF2 gamma, GTP-binding domain / Initiation factor eIF2 gamma, C-terminal / Initiation factor eIF2 gamma, C terminal / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 ...Cell division cycle protein 123 / D123 / Initiation factor eIF2 gamma, domain 2 / Initiation factor eIF2 gamma, GTP-binding domain / Initiation factor eIF2 gamma, C-terminal / Initiation factor eIF2 gamma, C terminal / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Translation protein, beta-barrel domain superfamily / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Eukaryotic translation initiation factor 2 subunit gamma / Translation initiation factor eIF2 assembly protein
Similarity search - Component
Biological speciesSchizosaccharomyces pombe (fission yeast)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsPanvert, M. / Dubiez, E. / Arnold, L. / Perez, J. / Seufert, W. / Mechulam, Y. / Schmitt, E.
Funding support France, 2items
OrganizationGrant numberCountry
CNRSUMR7654 France
Ecole PolytechniqueUMR7654 France
CitationJournal: Structure / Year: 2015
Title: Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features.
Authors: Panvert, M. / Dubiez, E. / Arnold, L. / Perez, J. / Mechulam, Y. / Seufert, W. / Schmitt, E.
History
DepositionApr 23, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Oct 14, 2015Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cell division cycle protein 123
B: Eukaryotic translation initiation factor 2 subunit gamma


Theoretical massNumber of molelcules
Total (without water)52,0872
Polymers52,0872
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1530 Å2
ΔGint-5 kcal/mol
Surface area20350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.000, 117.400, 132.350
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein Cell division cycle protein 123 / cdc123


Mass: 38979.051 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast)
Gene: cdc123, SPAP27G11.03 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / References: UniProt: Q9P7N5
#2: Protein Eukaryotic translation initiation factor 2 subunit gamma / eIF-2-gamma / eIF2gammaD3


Mass: 13108.387 Da / Num. of mol.: 1 / Fragment: UNP residues 410-527
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: GCD11, TIF213, YER025W / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / References: UniProt: P32481

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.8 Å3/Da / Density % sol: 56.02 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 25%PEG3350, 0.2M LISO4, 0.1M Tris pH 8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97857 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 12, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 3→45 Å / Num. obs: 12020 / % possible obs: 99.6 % / Redundancy: 7.3 % / Biso Wilson estimate: 101.91 Å2 / Rsym value: 0.102 / Net I/σ(I): 13.4
Reflection shellResolution: 3→3.17 Å / Redundancy: 7 % / Rmerge(I) obs: 1.15 / Mean I/σ(I) obs: 2 / % possible all: 97.8

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Processing

Software
NameVersionClassification
BUSTER2.10.1refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→45 Å / Cor.coef. Fo:Fc: 0.8912 / Cor.coef. Fo:Fc free: 0.8496 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 7.442 / SU Rfree Blow DPI: 0.37
RfactorNum. reflection% reflectionSelection details
Rfree0.2521 599 4.98 %RANDOM
Rwork0.2056 ---
obs0.2078 12018 99.89 %-
Displacement parametersBiso mean: 106.79 Å2
Baniso -1Baniso -2Baniso -3
1-7.9198 Å20 Å20 Å2
2---48.3451 Å20 Å2
3---40.4253 Å2
Refine analyzeLuzzati coordinate error obs: 0.624 Å
Refinement stepCycle: LAST / Resolution: 3→45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3032 0 0 0 3032
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.013102HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.184201HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1082SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes76HARMONIC2
X-RAY DIFFRACTIONt_gen_planes432HARMONIC5
X-RAY DIFFRACTIONt_it3102HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.8
X-RAY DIFFRACTIONt_other_torsion22.56
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion411SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact3407SEMIHARMONIC4
LS refinement shellResolution: 3→3.29 Å / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.3285 145 5.15 %
Rwork0.2618 2670 -
all0.2651 2815 -
obs--99.89 %
Refinement TLS params.

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

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.3450.3722-0.76910.85050.911611.37550.0202-0.21810.301-0.25620.0227-0.0663-1.3631-0.3415-0.0429-0.11380.13830.0661-0.19910.04950.01921.4361136.516139.086
23.81310.11-0.38710.9518-0.55935.620.1171-0.4054-0.01190.41560.14110.15960.9545-0.7773-0.2582-0.0642-0.1492-0.05830.09380.0851-0.142122.7278115.623164.512
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|* }
2X-RAY DIFFRACTION2{ B|* }

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