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- PDB-2e1r: Structure of eEF2 in complex with a sordarin derivative -

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Basic information

Entry
Database: PDB / ID: 2e1r
TitleStructure of eEF2 in complex with a sordarin derivative
ComponentsElongation factor 2EEF2
KeywordsTRANSLATION / protein-ligand complex / G-protein
Function / homology
Function and homology information


Peptide chain elongation / Synthesis of diphthamide-EEF2 / Protein methylation / positive regulation of translational elongation / translational elongation / translation elongation factor activity / Neutrophil degranulation / maintenance of translational fidelity / ribosome binding / ribonucleoprotein complex ...Peptide chain elongation / Synthesis of diphthamide-EEF2 / Protein methylation / positive regulation of translational elongation / translational elongation / translation elongation factor activity / Neutrophil degranulation / maintenance of translational fidelity / ribosome binding / ribonucleoprotein complex / chaperone binding / rRNA binding / GTPase activity / GTP binding / identical protein binding / cytosol
Similarity search - Function
Yeast translation eEF2 (G' domain) / Yeast translation eEF2 (G' domain) / Elongation Factor G (Translational Gtpase), domain 3 / Alpha-Beta Plaits - #240 / Elongation Factor G, domain II / Elongation Factor G, domain III / Elongation factor G, domain IV / Translation elongation factor EFG/EF2, domain IV / Elongation factor G, domain IV / Elongation factor G C-terminus ...Yeast translation eEF2 (G' domain) / Yeast translation eEF2 (G' domain) / Elongation Factor G (Translational Gtpase), domain 3 / Alpha-Beta Plaits - #240 / Elongation Factor G, domain II / Elongation Factor G, domain III / Elongation factor G, domain IV / Translation elongation factor EFG/EF2, domain IV / Elongation factor G, domain IV / Elongation factor G C-terminus / Elongation factor EFG, domain V-like / Elongation factor G C-terminus / Ribosomal Protein S5; domain 2 - #10 / EF-G domain III/V-like / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation factors / Ribosomal Protein S5; domain 2 / Elongation factor Tu domain 2 / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Translational (tr)-type GTP-binding domain / Elongation Factor Tu (Ef-tu); domain 3 / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / P-loop containing nucleotide triphosphate hydrolases / Alpha-Beta Plaits / Alpha-Beta Complex / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Chem-SOD / Elongation factor 2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (baker's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.15 Å
AuthorsSoe, R. / Mosley, R.T. / Andersen, G.R.
CitationJournal: J.Biol.Chem. / Year: 2007
Title: Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2
Authors: Soe, R. / Mosley, R.T. / Justice, M. / Nielsen-Kahn, J. / Shastry, M. / Merrill, A.R. / Andersen, G.R.
History
DepositionOct 27, 2006Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 14, 2006Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Elongation factor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,3693
Polymers93,4071
Non-polymers9622
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)116.860, 158.770, 60.310
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 Elongation factor 2 / EEF2 / EF-2 / Translation elongation factor 2 / Eukaryotic elongation factor 2 / eEF2 / Ribosomal translocase


Mass: 93407.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P32324
#2: Chemical ChemComp-SOD / (1S,4S,5S,6R,9S,11S)-6-CHLORO-9-FORMYL-13-ISOPROPYL-5-METHYL-2-({[(3AR,5R,7R ,7AS)-7-METHYL-3-METHYLENEHEXAHYDRO-2H-FURO[2,3-C]PYRAN-5-YL]OXY}METHYL)TETR ACYCLO[7.4.0.02,11.04,8]TRIDEC-12-ENE-1-CARBOXYLIC ACI


Mass: 519.069 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H39ClO6
#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM

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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: 2.99 Å3/Da / Density % sol: 58.91 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 7.2
Details: PEG8000, ethylene glycol, pH 7.2, VAPOR DIFFUSION, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, Hamburg / Beamline: BW7A / Wavelength: 0.9762 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Feb 26, 2003
RadiationMonochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 3.15→20 Å / Num. all: 20102 / Num. obs: 19727 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Rsym value: 0.07 / Net I/σ(I): 18
Reflection shellResolution: 3.15→3.34 Å / Redundancy: 3.5 % / Mean I/σ(I) obs: 4.2 / Num. unique all: 3193 / Rsym value: 0.32 / % possible all: 93

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Processing

Software
NameClassification
MAR345data collection
MOLREPphasing
CNSrefinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1n0u
Resolution: 3.15→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.27 957 -random
Rwork0.22 ---
all0.224 20102 --
obs0.224 19727 98.1 %-
Refinement stepCycle: LAST / Resolution: 3.15→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6446 0 64 0 6510
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.5
X-RAY DIFFRACTIONc_bond_d0.01

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