[English] 日本語
Yorodumi
- PDB-5y58: Crystal structure of Ku70/80 and TLC1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5y58
TitleCrystal structure of Ku70/80 and TLC1
Components
  • ATP-dependent DNA helicase II subunit 1
  • ATP-dependent DNA helicase II subunit 2
  • TLC1
KeywordsRNA BINDING PROTEIN / telomerase / telomere / protein-RNA complex
Function / homology
Function and homology information


donor selection / mitochondrial double-strand break repair via homologous recombination / subtelomeric heterochromatin formation => GO:0031509 / chromatin organization => GO:0006325 / : / protein localization to chromosome / establishment of protein-containing complex localization to telomere / Ku70:Ku80 complex / cellular response to X-ray / double-strand break repair via break-induced replication ...donor selection / mitochondrial double-strand break repair via homologous recombination / subtelomeric heterochromatin formation => GO:0031509 / chromatin organization => GO:0006325 / : / protein localization to chromosome / establishment of protein-containing complex localization to telomere / Ku70:Ku80 complex / cellular response to X-ray / double-strand break repair via break-induced replication / telomerase RNA binding / recombinational repair / silent mating-type cassette heterochromatin formation / telomeric DNA binding / subtelomeric heterochromatin formation / Neutrophil degranulation / DNA helicase activity / telomere maintenance / double-strand break repair via homologous recombination / cellular response to gamma radiation / double-strand break repair via nonhomologous end joining / nuclear envelope / chromatin organization / DNA helicase / damaged DNA binding / chromosome, telomeric region / ATP hydrolysis activity / DNA binding / ATP binding
Similarity search - Function
Ku70 / Ku80 / Ku70/Ku80 C-terminal arm / Ku70/Ku80, N-terminal alpha/beta / Ku70/Ku80 beta-barrel domain / Ku70/Ku80 C-terminal arm / Ku70/Ku80 N-terminal alpha/beta domain / Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen / Ku70/Ku80 beta-barrel domain / SPOC-like, C-terminal domain superfamily / von Willebrand factor A-like domain superfamily
Similarity search - Domain/homology
RNA / RNA (> 10) / ATP-dependent DNA helicase II subunit 1 / ATP-dependent DNA helicase II subunit 2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.8 Å
AuthorsChen, H. / Xue, J. / Wu, J. / Lei, M.
CitationJournal: Cell / Year: 2018
Title: Structural Insights into Yeast Telomerase Recruitment to Telomeres
Authors: Chen, H. / Xue, J. / Churikov, D. / Hass, E.P. / Shi, S. / Lemon, L.D. / Luciano, P. / Bertuch, A.A. / Zappulla, D.C. / Geli, V. / Wu, J. / Lei, M.
History
DepositionAug 8, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 20, 2017Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2018Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Mar 27, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_radiation_wavelength.wavelength

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: ATP-dependent DNA helicase II subunit 1
B: ATP-dependent DNA helicase II subunit 2
X: TLC1
C: ATP-dependent DNA helicase II subunit 1
D: ATP-dependent DNA helicase II subunit 2
Y: TLC1
E: ATP-dependent DNA helicase II subunit 1
F: ATP-dependent DNA helicase II subunit 2
Z: TLC1


Theoretical massNumber of molelcules
Total (without water)445,6259
Polymers445,6259
Non-polymers00
Water5,513306
1
A: ATP-dependent DNA helicase II subunit 1
B: ATP-dependent DNA helicase II subunit 2
X: TLC1


Theoretical massNumber of molelcules
Total (without water)148,5423
Polymers148,5423
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25560 Å2
ΔGint-160 kcal/mol
Surface area56270 Å2
MethodPISA
2
C: ATP-dependent DNA helicase II subunit 1
D: ATP-dependent DNA helicase II subunit 2
Y: TLC1


Theoretical massNumber of molelcules
Total (without water)148,5423
Polymers148,5423
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25560 Å2
ΔGint-160 kcal/mol
Surface area55790 Å2
MethodPISA
3
E: ATP-dependent DNA helicase II subunit 1
F: ATP-dependent DNA helicase II subunit 2
Z: TLC1


Theoretical massNumber of molelcules
Total (without water)148,5423
Polymers148,5423
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25560 Å2
ΔGint-160 kcal/mol
Surface area55930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.296, 115.159, 115.847
Angle α, β, γ (deg.)77.430, 78.480, 63.730
Int Tables number1
Space group name H-MP1

-
Components

#1: Protein ATP-dependent DNA helicase II subunit 1 / ATP-dependent DNA helicase II subunit Ku70 / High affinity DNA-binding factor subunit 1


Mass: 67709.078 Da / Num. of mol.: 3 / Fragment: UNP residues 28-602
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: YKU70, HDF1, NES24, YMR284W, YM8021.10 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): High Five / References: UniProt: P32807, DNA helicase
#2: Protein ATP-dependent DNA helicase II subunit 2 / ATP-dependent DNA helicase II subunit Ku80 / High affinity DNA-binding factor subunit 2 / Yeast Ku80


Mass: 71193.648 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: YKU80, HDF2, YMR106C, YM9718.05C / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): High Five / References: UniProt: Q04437, DNA helicase
#3: RNA chain TLC1


Mass: 9638.777 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: in vitro transcription
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Plasmid: pGlmS / Production host: Escherichia coli (E. coli)
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 306 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.03 Å3/Da / Density % sol: 59.35 % / Mosaicity: 0.487 °
Crystal growTemperature: 277 K / Method: evaporation / pH: 8
Details: 0.2 M calcium acetate, 0.1 M imidazole, 10% PEG8000

-
Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONSSRF BL18U110.97853
SYNCHROTRONSSRF BL19U120.97853
Detector
TypeIDDetectorDate
DECTRIS PILATUS 6M1PIXELMay 23, 2016
DECTRIS PILATUS 6M2PIXELMay 23, 2016
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray2
Radiation wavelength
IDWavelength (Å)Relative weight
10.978531
21
ReflectionResolution: 2.8→50 Å / Num. obs: 121941 / % possible obs: 93.9 % / Redundancy: 3.8 % / Biso Wilson estimate: 43.34 Å2 / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.045 / Rrim(I) all: 0.089 / Χ2: 0.881 / Net I/σ(I): 6.6 / Num. measured all: 463727
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.8-2.93.80.556125300.8030.3260.6450.88896
2.9-3.023.80.405123800.8720.2380.470.90295.7
3.02-3.153.90.269123820.9320.1570.3110.91495.2
3.15-3.323.80.194122810.9540.1130.2240.94594.7
3.32-3.533.80.136122440.9760.080.1580.97494.1
3.53-3.83.80.101120320.9810.060.1170.96192.8
3.8-4.183.70.072117970.9880.0430.0840.91990.9
4.18-4.793.60.059106240.9880.0360.0690.93781.8
4.79-6.033.90.051128080.9920.030.0590.75998.4
6.03-503.90.039128630.9960.0230.0460.65199.1

-
Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
HKL-3000data scaling
PDB_EXTRACT3.22data extraction
XDSphasing
RefinementMethod to determine structure: SAD / Resolution: 2.8→44.107 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 27.4 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2577 5877 4.97 %RANDOM
Rwork0.2153 112260 --
obs0.2175 118137 91.84 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 216.24 Å2 / Biso mean: 68.7218 Å2 / Biso min: 10.79 Å2
Refinement stepCycle: final / Resolution: 2.8→44.107 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27091 1923 0 306 29320
Biso mean---40.89 -
Num. residues----3427
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00329841
X-RAY DIFFRACTIONf_angle_d0.58740713
X-RAY DIFFRACTIONf_chiral_restr0.0244647
X-RAY DIFFRACTIONf_plane_restr0.0024869
X-RAY DIFFRACTIONf_dihedral_angle_d12.4211673
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.8001-2.83190.35151410.29082887302869
2.8319-2.86520.36531430.27893175331879
2.8652-2.90010.34341690.27023637380688
2.9001-2.93680.31351770.27313729390692
2.9368-2.97540.3132110.27563859407094
2.9754-3.01620.36971910.29123823401495
3.0162-3.05930.35181990.27353885408494
3.0593-3.10490.35932220.25363797401995
3.1049-3.15340.27522140.24323904411896
3.1534-3.20510.33162160.24143851406794
3.2051-3.26040.28952010.24033853405495
3.2604-3.31960.30271950.23843860405594
3.3196-3.38350.31311860.23073833401994
3.3835-3.45250.26462080.23023823403194
3.4525-3.52750.2691910.23333843403494
3.5275-3.60960.28611870.22533846403393
3.6096-3.69980.22411630.21373761392493
3.6998-3.79980.26251930.21073746393992
3.7998-3.91150.2382130.20753699391291
3.9115-4.03770.2391980.20453684388290
4.0377-4.18190.23521810.19623729391091
4.1819-4.34920.24582050.1943571377688
4.3492-4.54690.21081800.1913308348882
4.5469-4.78640.21741610.18153052321375
4.7864-5.08590.21021960.1734026422298
5.0859-5.47790.21352290.18434026425599
5.4779-6.02790.26332330.20634002423599
6.0279-6.89730.2592240.21434027425199
6.8973-8.6790.22892370.19834021425899
8.679-44.11240.19242130.18654003421698
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)
11.8314-0.6886-0.30431.16210.61841.3945-0.2563-0.53650.12620.26780.2031-0.26830.02390.09140.04650.17710.0847-0.10210.32230.0070.25240.34190.0994134.8163
21.89120.0858-0.16591.96240.20031.0145-0.190.3796-0.4235-0.61160.1451-0.52740.34880.15230.02460.3250.04590.17930.2721-0.09390.43289.540471.9823105.1682
32.7175-0.1475-1.27564.06140.97531.924-0.2983-0.0691-0.0173-0.02530.11960.38250.0065-0.27020.21010.48740.002-0.00770.2631-0.08260.3986-6.732572.3535106.0173
41.42280.23760.1631.47360.71481.225-0.05620.01420.1141-0.0039-0.12680.2947-0.1069-0.1680.09490.1592-0.0005-0.00240.13360.00380.261-59.29118.5053121.3165
51.2713-0.12360.23681.47130.08551.5609-0.0795-0.28030.40860.33010.0317-0.3937-0.4270.457-0.07230.3891-0.1159-0.11740.3234-0.14380.4732-29.8718132.9884136.0446
61.15261.61161.16994.59290.272.1357-0.0547-0.1584-0.0617-0.215-0.0471-0.04290.2724-0.04170.11350.39980.0912-0.0820.5189-0.06340.2656-27.2232117.0481134.1851
71.356-0.70610.2791.0368-0.16331.37090.15220.8884-0.8769-0.0917-0.0530.06570.43470.1837-0.09020.298-0.1129-0.1460.4498-0.60980.6939-37.926365.844585.3757
82.0244-0.1185-0.00471.07960.09132.10930.22471.04170.1582-0.1347-0.0350.5556-0.3903-0.53720.04950.28310.0568-0.12510.8101-0.11550.3452-60.146892.637576.3165
94.6758-0.70260.39911.2636-2.13233.75810.25350.0953-0.45960.1619-0.10840.1009-0.13810.2302-0.13750.2605-0.08490.0470.4863-0.18490.4518-56.646394.145692.1351
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain AA28 - 584
2X-RAY DIFFRACTION2chain BB2 - 621
3X-RAY DIFFRACTION3chain XX286 - 315
4X-RAY DIFFRACTION4chain CC28 - 584
5X-RAY DIFFRACTION5chain DD2 - 621
6X-RAY DIFFRACTION6chain YY286 - 315
7X-RAY DIFFRACTION7chain EE28 - 584
8X-RAY DIFFRACTION8chain FF2 - 621
9X-RAY DIFFRACTION9chain ZZ286 - 315

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more