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- PDB-5ol8: Structure of human mitochondrial transcription elongation factor ... -

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Basic information

Entry
Database: PDB / ID: 5ol8
TitleStructure of human mitochondrial transcription elongation factor (TEFM) C-terminal domain
ComponentsTranscription elongation factor, mitochondrial
KeywordsTRANSCRIPTION / Elongation Factor / Mitochondria / Resolvase / RNA Polymerase
Function / homology
Function and homology information


transcription elongation by mitochondrial RNA polymerase / mitochondrial transcription / oxidative phosphorylation / DNA polymerase processivity factor activity / mitochondrial nucleoid / mitochondrial matrix / ribonucleoprotein complex / mitochondrion / RNA binding
Similarity search - Function
Transcription elongation factor, mitochondrial / Helix-hairpin-helix motif / RuvA domain 2-like / Ribonuclease H superfamily / Ribonuclease H-like superfamily
Similarity search - Domain/homology
Transcription elongation factor, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.9 Å
AuthorsHillen, H.S. / Parshin, A.V. / Agaronyan, K. / Morozov, Y. / Graber, J.J. / Chernev, A. / Schwinghammer, K. / Urlaub, H. / Anikin, M. / Cramer, P. / Temiakov, D.
Funding support United States, Germany, 5items
OrganizationGrant numberCountry
National Institutes of HealthRO1 GM104231 United States
German Research FoundationSFB860 Germany
German Research FoundationSPP1935 Germany
European Research Council693023 Germany
Volkswagen Foundation Germany
CitationJournal: Cell / Year: 2017
Title: Mechanism of Transcription Anti-termination in Human Mitochondria.
Authors: Hillen, H.S. / Parshin, A.V. / Agaronyan, K. / Morozov, Y.I. / Graber, J.J. / Chernev, A. / Schwinghammer, K. / Urlaub, H. / Anikin, M. / Cramer, P. / Temiakov, D.
History
DepositionJul 27, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 18, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 25, 2017Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Nov 29, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
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: Transcription elongation factor, mitochondrial
B: Transcription elongation factor, mitochondrial
C: Transcription elongation factor, mitochondrial
D: Transcription elongation factor, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)149,1208
Polymers148,7514
Non-polymers3684
Water2,324129
1
A: Transcription elongation factor, mitochondrial
B: Transcription elongation factor, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,5604
Polymers74,3762
Non-polymers1842
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2890 Å2
ΔGint-25 kcal/mol
Surface area19950 Å2
MethodPISA
2
C: Transcription elongation factor, mitochondrial
D: Transcription elongation factor, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,5604
Polymers74,3762
Non-polymers1842
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2840 Å2
ΔGint-25 kcal/mol
Surface area20210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.480, 112.540, 88.840
Angle α, β, γ (deg.)90.00, 110.13, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11D-527-

HOH

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Components

#1: Protein
Transcription elongation factor, mitochondrial


Mass: 37187.785 Da / Num. of mol.: 4 / Fragment: UNP Residues 51-360
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TEFM, C17orf42 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2 / References: UniProt: Q96QE5
#2: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C3H8O3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 129 / 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: 2.12 Å3/Da / Density % sol: 42.1 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: Limited proteolysis with ArgC at RT for 20min. BIS-TRIS pH 5.5-6.5, MgCl2, PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.0, 0.9765
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 24, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
111
20.97651
ReflectionResolution: 1.9→46.233 Å / Num. obs: 70199 / % possible obs: 98.1 % / Redundancy: 6.6 % / CC1/2: 1 / Rmerge(I) obs: 0.051 / Net I/σ(I): 17.92
Reflection shellResolution: 1.9→1.94 Å / Redundancy: 5.04 % / Rmerge(I) obs: 2.49 / Mean I/σ(I) obs: 0.79 / Num. unique obs: 4740 / CC1/2: 0.35 / % possible all: 89.5

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
XSCALEdata scaling
AutoSolphasing
RefinementMethod to determine structure: SAD / Resolution: 1.9→46.233 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 34.34
RfactorNum. reflection% reflection
Rfree0.2278 3503 5 %
Rwork0.1954 --
obs0.197 70119 98.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.9→46.233 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6724 0 24 129 6877
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0036888
X-RAY DIFFRACTIONf_angle_d0.5069276
X-RAY DIFFRACTIONf_dihedral_angle_d15.4744156
X-RAY DIFFRACTIONf_chiral_restr0.0411036
X-RAY DIFFRACTIONf_plane_restr0.0021156
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.9260.46331250.48292406X-RAY DIFFRACTION88
1.926-1.95350.51731280.45382439X-RAY DIFFRACTION91
1.9535-1.98270.41051360.43152575X-RAY DIFFRACTION95
1.9827-2.01360.45051420.42792701X-RAY DIFFRACTION99
2.0136-2.04670.41131420.38142688X-RAY DIFFRACTION99
2.0467-2.08190.36141410.35182683X-RAY DIFFRACTION99
2.0819-2.11980.35811400.30422672X-RAY DIFFRACTION99
2.1198-2.16060.30731410.28322675X-RAY DIFFRACTION99
2.1606-2.20470.30371420.29072695X-RAY DIFFRACTION99
2.2047-2.25260.36571400.27042660X-RAY DIFFRACTION99
2.2526-2.3050.2931400.26192649X-RAY DIFFRACTION98
2.305-2.36270.30911410.24732680X-RAY DIFFRACTION99
2.3627-2.42650.29621430.23472717X-RAY DIFFRACTION99
2.4265-2.49790.26991410.23682702X-RAY DIFFRACTION99
2.4979-2.57850.28141410.22732694X-RAY DIFFRACTION99
2.5785-2.67070.26261420.22642699X-RAY DIFFRACTION99
2.6707-2.77760.25781410.20892666X-RAY DIFFRACTION98
2.7776-2.9040.28381400.21872664X-RAY DIFFRACTION98
2.904-3.05710.22151420.21582706X-RAY DIFFRACTION100
3.0571-3.24860.23341430.20322710X-RAY DIFFRACTION100
3.2486-3.49930.21691420.19042692X-RAY DIFFRACTION99
3.4993-3.85130.20661390.17562670X-RAY DIFFRACTION98
3.8513-4.40820.21081440.1482735X-RAY DIFFRACTION100
4.4082-5.55240.16031410.14242685X-RAY DIFFRACTION98
5.5524-46.24640.17231460.1592753X-RAY DIFFRACTION99
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)
10.72320.9535-0.09891.48160.11560.29280.3742-1.05930.48910.8964-0.35390.7183-0.4451-0.6585-0.00460.8989-0.08570.12620.9508-0.01840.5803-4.663998.2854-10.5554
22.58351.22420.29532.34760.67920.13620.4668-0.1726-0.40270.30890.1791-0.7642-0.49610.2852-0.00090.443-0.049-0.01930.47720.04880.55849.631697.6402-23.3098
31.25631.02780.38033.0229-0.45940.38820.4199-0.0623-0.18690.6592-0.1184-0.98210.3892-0.11460.00020.541-0.1497-0.14390.6940.05910.946714.575499.1151-17.1483
40.38630.0673-0.25370.3877-0.17120.12690.25870.3315-1.1768-0.3773-0.026-0.17740.20570.436700.787-0.03570.1120.70440.01080.63098.444991.56-40.1461
51.00310.8039-0.31763.79442.21233.96670.0214-0.06020.03380.14890.028-0.56-0.1378-0.14570.00050.4512-0.0149-0.01440.50790.06240.57523.931792.5795-26.9882
62.84821.4824-0.88381.59150.86331.9655-0.32240.08260.3601-0.70490.41160.2288-0.747-0.11040.00080.5869-0.0832-0.02840.44180.04480.5062-0.943694.3576-32.8903
73.00390.79340.0761.33191.35411.7330.1911-0.30870.30790.4828-0.20570.3169-0.2908-0.36510.00020.6001-0.0091-0.03230.57170.00460.495-0.0503102.0365-20.9425
80.50030.61940.37560.47530.47820.49490.0529-0.51920.35470.81470.217-0.6562-1.37750.65130.00320.9735-0.2355-0.14840.80180.00671.050717.6997112.2832-14.2379
90.6762-1.13720.68473.9366-0.26151.58180.08170.3947-0.1611-0.64960.2611-2.4534-0.07261.16630.0090.5337-0.20990.02750.8215-0.09161.36822.5923104.6868-23.3348
101.90011.23061.46713.52110.64191.2373-0.0195-0.10790.28570.3086-0.0587-0.295-0.4886-0.7976-0.00020.6072-0.0592-0.11160.53090.01870.57176.4201105.2921-17.1265
112.55691.59511.76883.95610.65534.53530.26640.0198-0.5881-0.32-0.1106-0.21360.7481-0.021500.5528-0.02390.00970.47420.01930.5562-5.777169.3206-37.1827
120.1203-0.3294-0.31840.44730.40230.438-0.3518-0.93530.5758-0.1447-0.22031.49260.1582-1.1929-0.00050.64170.04910.01090.8684-0.07290.7251-17.434988.1526-29.7497
131.61041.32231.51183.07281.77292.6501-0.068-0.02410.0584-0.3597-0.0336-0.1186-0.0598-0.2514-0.00010.4289-0.03580.03070.45370.02770.4662-7.118283.1681-34.0064
143.09011.7195-0.38892.53061.78341.79320.04510.5696-0.3637-0.35360.0298-0.03960.19360.16910.00050.5388-0.0194-0.01830.4920.03390.5277-4.903474.6645-43.2593
150.10560.69220.74030.69470.82470.5680.14760.1446-0.20740.0814-0.37890.17350.2006-0.6319-0.00010.7913-0.1529-0.09210.7831-0.03920.7581-19.534458.9408-44.8637
163.14872.38762.27874.43440.52476.06970.1128-0.38490.07190.1871-0.26340.23180.5664-1.2165-0.00010.5568-0.144-0.01250.6647-0.03630.5552-17.15667.1775-39.1044
174.10040.2108-0.36284.8222-2.57783.77180.0554-0.19390.3260.3398-0.20080.0205-0.6025-0.0190.00010.5454-0.00340.02640.5041-0.00630.4969-39.9717131.92-79.045
181.9015-0.33840.2371.9711-0.54161.18630.09521.3336-0.1123-1.8336-0.149-0.08090.58760.91070.00030.812-0.01090.09280.76050.1250.6891-28.4825115.7493-84.2622
192.6866-2.41080.46653.2491-2.2592.78190.2454-0.25070.1375-0.2216-0.19360.1703-0.0469-0.2278-00.4872-0.03370.02730.49980.05620.4891-38.9986119.8194-75.9279
201.844-1.13190.72891.3116-2.29853.15140.14150.13260.1523-0.42580.0610.3222-0.1055-0.50870.00010.68970.0613-0.01140.60430.00670.5861-48.0434134.3282-90.3321
212.8668-0.46880.39674.3626-2.60223.33520.27360.3030.0305-0.3986-0.4101-0.14230.18020.101800.54450.07130.06320.49950.03830.4913-39.5921133.7314-90.5976
223.7025-1.77032.26376.0322-0.17893.1563-0.13-0.00530.11740.24580.0326-0.8145-0.00860.1258-0.00390.497-0.0569-0.0130.56630.06390.5599-22.5177102.9984-63.1136
233.1689-2.23281.59935.9613-2.1392.3118-0.1483-0.42020.0920.40380.25670.1330.1401-0.2611-0.00040.5691-0.06180.05550.60430.03160.4622-36.0846108.7201-66.1244
242.4406-1.89641.77544.2536-2.13712.8496-0.00320.04840.1072-0.2459-0.0557-0.3257-0.03180.2048-0.00020.4937-0.07270.06360.50280.06060.4836-29.5118106.4308-71.9015
253.0705-2.0221-1.18382.10820.47550.87210.1099-0.7205-0.83940.23490.1039-0.54620.8152-0.2183-00.9108-0.161-0.08520.79760.22690.7321-25.510188.0803-56.4039
263.57260.89832.28382.90381.8672.38690.2012-1.7850.40261.0361-0.2070.56560.0161-1.15-0.13421.0007-0.1645-0.01861.39380.12050.4478-33.45196.5089-48.564
270.6796-0.21111.24443.17530.09012.09080.26960.1034-0.08310.1536-0.0972-0.39090.0637-0.0292-0.00020.49530.0116-0.05120.5320.05530.5073-23.053696.0617-62.5471
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 153 through 168 )
2X-RAY DIFFRACTION2chain 'A' and (resid 169 through 186 )
3X-RAY DIFFRACTION3chain 'A' and (resid 187 through 198 )
4X-RAY DIFFRACTION4chain 'A' and (resid 199 through 208 )
5X-RAY DIFFRACTION5chain 'A' and (resid 209 through 240 )
6X-RAY DIFFRACTION6chain 'A' and (resid 241 through 261 )
7X-RAY DIFFRACTION7chain 'A' and (resid 262 through 296 )
8X-RAY DIFFRACTION8chain 'A' and (resid 297 through 318 )
9X-RAY DIFFRACTION9chain 'A' and (resid 319 through 337 )
10X-RAY DIFFRACTION10chain 'A' and (resid 338 through 357 )
11X-RAY DIFFRACTION11chain 'B' and (resid 153 through 196 )
12X-RAY DIFFRACTION12chain 'B' and (resid 197 through 208 )
13X-RAY DIFFRACTION13chain 'B' and (resid 209 through 261 )
14X-RAY DIFFRACTION14chain 'B' and (resid 262 through 296 )
15X-RAY DIFFRACTION15chain 'B' and (resid 297 through 318 )
16X-RAY DIFFRACTION16chain 'B' and (resid 319 through 357 )
17X-RAY DIFFRACTION17chain 'C' and (resid 153 through 196 )
18X-RAY DIFFRACTION18chain 'C' and (resid 197 through 222 )
19X-RAY DIFFRACTION19chain 'C' and (resid 223 through 272 )
20X-RAY DIFFRACTION20chain 'C' and (resid 273 through 318 )
21X-RAY DIFFRACTION21chain 'C' and (resid 319 through 357 )
22X-RAY DIFFRACTION22chain 'D' and (resid 153 through 196 )
23X-RAY DIFFRACTION23chain 'D' and (resid 197 through 240 )
24X-RAY DIFFRACTION24chain 'D' and (resid 241 through 284 )
25X-RAY DIFFRACTION25chain 'D' and (resid 285 through 318 )
26X-RAY DIFFRACTION26chain 'D' and (resid 319 through 337 )
27X-RAY DIFFRACTION27chain 'D' and (resid 338 through 357 )

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