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- PDB-4pc2: Elongation factor Tu:Ts complex with a bound GDP -

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Basic information

Entry
Database: PDB / ID: 4pc2
TitleElongation factor Tu:Ts complex with a bound GDP
Components(Elongation factor ...) x 2
KeywordsTRANSLATION / G:GEF:GDP complex / Elongation Factor Tu / Elongation factor Ts
Function / homology
Function and homology information


guanosine tetraphosphate binding / translation elongation factor activity / GTPase activity / GTP binding / cytosol / cytoplasm
Similarity search - Function
GTP Cyclohydrolase I; Chain A, domain 1 - #20 / Elongation factor Ts, dimerisation domain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / GTP Cyclohydrolase I; Chain A, domain 1 ...GTP Cyclohydrolase I; Chain A, domain 1 - #20 / Elongation factor Ts, dimerisation domain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / GTP Cyclohydrolase I; Chain A, domain 1 / Tetrahydropterin Synthase; Chain A / Ubiquitin-associated (UBA) domain / Translation elongation factor EFTu/EF1A, C-terminal / Translation elongation factor EFTu/EF1A, bacterial/organelle / Elongation factor Tu, domain 2 / Elongation factor Tu (EF-Tu), GTP-binding domain / : / Elongation factor Tu C-terminal domain / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / UBA-like superfamily / Translation factors / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Helicase, Ruva Protein; domain 3 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Elongation factor Tu / : / Elongation factor Ts
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1999 Å
AuthorsThirup, S.S.
CitationJournal: J.Struct.Biol. / Year: 2015
Title: Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.
Authors: Thirup, S.S. / Van, L.B. / Nielsen, T.K. / Knudsen, C.R.
History
DepositionApr 14, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 6, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 1, 2015Group: Database references
Revision 1.2Jul 15, 2015Group: Database references
Revision 1.3Mar 7, 2018Group: Database references / Derived calculations / Source and taxonomy
Category: citation / entity_src_gen / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Sep 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Elongation factor Tu
C: Elongation factor Ts
B: Elongation factor Tu
D: Elongation factor Ts
hetero molecules


Theoretical massNumber of molelcules
Total (without water)148,59413
Polymers147,3474
Non-polymers1,2489
Water12,773709
1
A: Elongation factor Tu
C: Elongation factor Ts
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,3727
Polymers73,6732
Non-polymers6985
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4690 Å2
ΔGint-51 kcal/mol
Surface area29690 Å2
MethodPISA
2
B: Elongation factor Tu
D: Elongation factor Ts
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,2236
Polymers73,6732
Non-polymers5504
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4850 Å2
ΔGint-63 kcal/mol
Surface area30340 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.927, 108.510, 193.750
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Elongation factor ... , 2 types, 4 molecules ABCD

#1: Protein Elongation factor Tu / EF-Tu


Mass: 43340.465 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / DH10B / Gene: tufA, tuf, ECDH10B_3514 / Production host: Escherichia coli (E. coli) / References: UniProt: B1X6I9, UniProt: A0A0M3KKV1*PLUS
#2: Protein Elongation factor Ts / EF-Ts


Mass: 30332.795 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: tsf, BN17_45931, ECs0172, LF82_2325 / Production host: Escherichia coli (E. coli) / References: UniProt: C3TPM7

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Non-polymers , 4 types, 718 molecules

#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 709 / 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: 2.63 Å3/Da / Density % sol: 53.27 %
Crystal growTemperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 100mM Hepes 73 mM Tris 17% PEG 6000 5% glycerol 150mM NaCl 1mM GDP 5mM EDTA

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 0.944 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Apr 22, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.944 Å / Relative weight: 1
ReflectionResolution: 2.1999→35 Å / Num. obs: 78193 / % possible obs: 97.8 % / Redundancy: 5 % / Rmerge(I) obs: 0.044 / Net I/σ(I): 18.1
Reflection shellResolution: 2.1999→2.28 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.252 / Mean I/σ(I) obs: 4.2 / % possible all: 85.3

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Processing

SoftwareName: PHENIX / Version: (phenix.refine: dev_1593) / Classification: refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4PC1
Resolution: 2.1999→34.989 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1 / Phase error: 19.45 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2136 4290 5.62 %random
Rwork0.1652 ---
obs0.1679 76340 95.55 %-
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.1999→34.989 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9895 0 73 709 10677
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0110155
X-RAY DIFFRACTIONf_angle_d1.14913717
X-RAY DIFFRACTIONf_dihedral_angle_d14.5433827
X-RAY DIFFRACTIONf_chiral_restr0.0441577
X-RAY DIFFRACTIONf_plane_restr0.0051779
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1999-2.22490.22751040.2111694X-RAY DIFFRACTION68
2.2249-2.25110.21231070.18362054X-RAY DIFFRACTION82
2.2511-2.27860.21791290.18492105X-RAY DIFFRACTION86
2.2786-2.30740.23141260.18922216X-RAY DIFFRACTION88
2.3074-2.33770.25191340.1862298X-RAY DIFFRACTION93
2.3377-2.36980.23911270.17512333X-RAY DIFFRACTION93
2.3698-2.40360.21471380.17782335X-RAY DIFFRACTION94
2.4036-2.43950.2491470.1812380X-RAY DIFFRACTION95
2.4395-2.47760.22021530.1782340X-RAY DIFFRACTION95
2.4776-2.51820.2121550.18152387X-RAY DIFFRACTION96
2.5182-2.56160.22331630.17662356X-RAY DIFFRACTION96
2.5616-2.60820.2451700.18252364X-RAY DIFFRACTION97
2.6082-2.65830.2431640.18442427X-RAY DIFFRACTION97
2.6583-2.71260.22861350.17762422X-RAY DIFFRACTION97
2.7126-2.77150.23671510.18232435X-RAY DIFFRACTION98
2.7715-2.8360.22591920.18542423X-RAY DIFFRACTION98
2.836-2.90690.26021460.18392449X-RAY DIFFRACTION99
2.9069-2.98540.25131760.18042439X-RAY DIFFRACTION99
2.9854-3.07320.25551600.18472480X-RAY DIFFRACTION99
3.0732-3.17230.19591540.18262468X-RAY DIFFRACTION99
3.1723-3.28560.22731770.1742479X-RAY DIFFRACTION99
3.2856-3.41710.23932190.17032411X-RAY DIFFRACTION100
3.4171-3.57250.20331550.16182521X-RAY DIFFRACTION100
3.5725-3.76060.21411290.15542550X-RAY DIFFRACTION100
3.7606-3.99590.20161160.15472535X-RAY DIFFRACTION99
3.9959-4.30390.19111220.1432561X-RAY DIFFRACTION100
4.3039-4.73610.14111030.1272591X-RAY DIFFRACTION100
4.7361-5.41920.18371000.13922614X-RAY DIFFRACTION100
5.4192-6.81940.18561150.17262637X-RAY DIFFRACTION100
6.8194-34.99350.1751230.15432746X-RAY DIFFRACTION100
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)
12.16360.5407-0.18724.7025-2.16912.5023-0.36010.0602-0.3494-0.29470.41450.02210.3435-0.2757-0.05780.429-0.05380.06270.4343-0.02590.335559.5898-6.066472.9857
21.20330.4078-0.08021.9512-1.31932.5302-0.0226-0.3202-0.15420.1132-0.05750.02470.05140.04070.06670.21540.07610.02530.32290.03020.273945.753317.408694.1794
32.8634-0.2282-2.71363.99971.62813.119-0.2735-0.48120.12480.87980.4729-0.19990.75220.8913-0.21830.49270.13030.07580.5784-0.090.409481.4494-6.863157.1729
44.4164-5.64180.17417.3646-0.16320.53530.67250.04380.1589-0.6749-0.2292-0.4438-0.08990.4262-0.39630.42270.01220.05520.3852-0.12530.313375.0029-0.351148.6022
51.49771.4013-0.36666.9712-1.33111.062-0.06630.172-0.09720.29740.0835-0.09970.0374-0.0346-0.00660.1952-0.01860.01460.2143-0.04690.213466.703120.182755.7559
61.1611-1.007-0.56636.31451.59482.3368-0.0250.05220.0023-0.12530.1199-0.14210.02250.1554-0.08820.1026-0.0538-0.01940.2504-0.030.20865.556222.87253.9511
78.04630.90256.06833.60760.08059.4711-0.04880.22980.20390.13450.05280.1309-0.33570.19930.03790.19990.00240.08370.2012-0.00540.226654.024738.780858.9632
85.41565.4771-6.79137.4112-5.95339.3445-0.09090.80310.0463-0.4329-0.01820.06940.1787-0.14090.1050.40480.0867-0.06230.3874-0.01020.288331.160636.728847.0925
96.42250.9667-1.24414.39331.89361.5840.34610.46580.3908-0.3205-0.04060.0572-0.3213-0.1893-0.23260.39710.01060.03910.3720.07440.292830.06342.246452.9809
103.57360.7017-0.52544.09030.15223.80270.1013-0.07430.370.0933-0.0016-0.0073-0.5208-0.0705-0.09620.208-0.01940.0290.17610.0040.236353.164942.054261.6846
113.03915.0657-2.77038.48-4.60232.5317-0.0404-0.3494-0.2895-1.00390.4620.87890.7678-0.6988-0.35210.5559-0.1959-0.22890.53560.21370.625647.77813.108660.2431
120.71620.5328-0.56754.6049-0.24691.6315-0.07180.21210.0171-0.01180.0145-0.671-0.08880.33310.04080.3926-0.1052-0.03850.4050.01820.493134.662267.36478.2806
134.93361.05211.03514.29040.49253.5648-0.1274-0.0280.7170.01-0.07410.4326-0.4385-0.20850.13030.4181-0.0129-0.02930.3241-0.03020.398819.806474.400880.2151
142.03920.78350.6912.52640.62552.07510.1137-0.37660.15840.3715-0.1091-0.2265-0.03140.11060.01020.2383-0.0178-0.01730.3357-0.0060.290544.128647.162295.023
156.924-6.2590.01937.3685-0.99292.2368-0.6116-0.75341.24930.30930.20070.3537-0.7985-0.62720.20980.58390.1753-0.15910.5413-0.10620.90770.411276.504271.3408
164.1559-5.5937-2.12588.69881.92458.0345-0.0801-0.22460.4699-0.26210.12590.5679-0.6885-0.6446-0.08140.43-0.0024-0.1080.35790.06790.42211.881568.632662.0424
172.96611.20970.68144.25041.40221.2201-0.03520.0191-0.04360.20960.0206-0.0558-0.0006-0.05370.00380.2165-0.0299-0.02290.1830.04260.152810.773846.410566.548
181.7092-1.94630.627.245-1.44461.9962-0.08390.0248-0.125-0.09030.17060.363-0.0109-0.1028-0.07460.1546-0.03940.03720.2510.04210.187511.437643.615664.3314
196.11950.4777-2.81074.6416-0.40564.6928-0.0769-0.0559-0.60580.08730.0268-0.00640.1492-0.1540.08840.1630.0103-0.02960.18610.01010.315123.062327.125564.5632
203.31773.06551.28763.0170.76582.6159-0.12521.3481-0.3754-0.22140.1916-0.0777-0.06380.0269-0.04390.41420.04790.03840.4398-0.0490.305241.778628.880145.5625
219.1865-0.3795-6.92745.2084-1.59087.47990.270.6173-0.5989-0.1807-0.11120.09950.6075-0.3599-0.14630.41080.0302-0.12380.4268-0.08330.391542.161823.075850.9399
223.35550.17250.32173.6762-0.67513.64180.124-0.1224-0.67880.0604-0.0495-0.09610.43530.1543-0.06340.2157-0.0039-0.01050.19680.01120.297324.789123.870966.8093
232.64523.40912.27334.38982.92721.9509-0.43840.3228-0.1843-1.08930.5861-1.0698-0.62520.8785-0.12450.5472-0.2130.14250.6309-0.00790.488631.817961.4563.7186
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 8:198)
2X-RAY DIFFRACTION2chain 'A' and (resseq 199:393)
3X-RAY DIFFRACTION3chain 'C' and (resseq 1:32)
4X-RAY DIFFRACTION4chain 'C' and (resseq 33:51)
5X-RAY DIFFRACTION5chain 'C' and (resseq 52:106)
6X-RAY DIFFRACTION6chain 'C' and (resseq 107:161)
7X-RAY DIFFRACTION7chain 'C' and (resseq 162:186)
8X-RAY DIFFRACTION8chain 'C' and (resseq 187:204)
9X-RAY DIFFRACTION9chain 'C' and (resseq 205:225)
10X-RAY DIFFRACTION10chain 'C' and (resseq 226:259)
11X-RAY DIFFRACTION11chain 'C' and (resseq 260:282)
12X-RAY DIFFRACTION12chain 'B' and (resseq 8:106)
13X-RAY DIFFRACTION13chain 'B' and (resseq 107:198)
14X-RAY DIFFRACTION14chain 'B' and (resseq 199:393)
15X-RAY DIFFRACTION15chain 'D' and (resseq 1:32)
16X-RAY DIFFRACTION16chain 'D' and (resseq 33:51)
17X-RAY DIFFRACTION17chain 'D' and (resseq 52:106)
18X-RAY DIFFRACTION18chain 'D' and (resseq 107:161)
19X-RAY DIFFRACTION19chain 'D' and (resseq 162:186)
20X-RAY DIFFRACTION20chain 'D' and (resseq 187:207)
21X-RAY DIFFRACTION21chain 'D' and (resseq 208:225)
22X-RAY DIFFRACTION22chain 'D' and (resseq 226:259)
23X-RAY DIFFRACTION23chain 'D' and (resseq 260:282)

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