[English] 日本語
Yorodumi
- PDB-7cuh: Crystal structure of fission yeast Pot1 and ssDNA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7cuh
TitleCrystal structure of fission yeast Pot1 and ssDNA
Components
  • Protection of telomeres protein 1
  • Telomere single-strand DNA
KeywordsDNA BINDING PROTEIN / telomere / protein-ssDNA complex
Function / homology
Function and homology information


Removal of the Flap Intermediate from the C-strand / telomere cap complex / chromosome, telomeric repeat region / telomerase inhibitor activity / shelterin complex / regulation of telomere maintenance via telomerase / telomere capping / single-stranded telomeric DNA binding / nuclear telomere cap complex / G-rich strand telomeric DNA binding ...Removal of the Flap Intermediate from the C-strand / telomere cap complex / chromosome, telomeric repeat region / telomerase inhibitor activity / shelterin complex / regulation of telomere maintenance via telomerase / telomere capping / single-stranded telomeric DNA binding / nuclear telomere cap complex / G-rich strand telomeric DNA binding / telomere maintenance / nucleus / cytosol
Similarity search - Function
Protection of telomeres protein 1, ssDNA-binding domain / ssDNA-binding domain of telomere protection protein / Protection of telomeres protein 1 / Telomeric single stranded DNA binding POT1/Cdc13 / Telomeric single stranded DNA binding POT1/CDC13 / Telomeric single stranded DNA binding POT1/CDC13 / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
DNA / DNA (> 10) / Protection of telomeres protein 1
Similarity search - Component
Biological speciesSchizosaccharomyces pombe (fission yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsSun, H. / Wu, Z. / Wu, J. / Lei, M.
CitationJournal: Plos Genet. / Year: 2022
Title: Structural insights into Pot1-ssDNA, Pot1-Tpz1 and Tpz1-Ccq1 Interactions within fission yeast shelterin complex.
Authors: Sun, H. / Wu, Z. / Zhou, Y. / Lu, Y. / Lu, H. / Chen, H. / Shi, S. / Zeng, Z. / Wu, J. / Lei, M.
History
DepositionAug 23, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 25, 2021Provider: repository / Type: Initial release
Revision 1.1Sep 7, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _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 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Protection of telomeres protein 1
B: Telomere single-strand DNA


Theoretical massNumber of molelcules
Total (without water)45,1442
Polymers45,1442
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3890 Å2
ΔGint-18 kcal/mol
Surface area17270 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.212, 65.903, 92.789
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Protection of telomeres protein 1


Mass: 39516.605 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast)
Strain: 972 / ATCC 24843 / Gene: pot1, SPAC26H5.06 / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O13988
#2: DNA chain Telomere single-strand DNA


Mass: 5627.637 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Schizosaccharomyces pombe (fission yeast)

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.62 %
Crystal growTemperature: 277 K / Method: evaporation / pH: 5.5
Details: 20% PEG3350, 100 mM ammonium sulfate and 100 mM Bis-Tris

-
Data collection

Diffraction
IDMean temperature (K)Crystal-IDSerial crystal experiment
11001N
21001N
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONSSRF BL18U110.97791
SYNCHROTRONSSRF BL19U120.97853
Detector
TypeIDDetectorDate
DECTRIS PILATUS3 6M1PIXELMar 16, 2016
DECTRIS PILATUS 6M2PIXELMar 16, 2016
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray2
Radiation wavelength
IDWavelength (Å)Relative weight
10.977911
20.978531
ReflectionResolution: 3→50 Å / Num. obs: 8002 / % possible obs: 99.3 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.137 / Rpim(I) all: 0.059 / Rrim(I) all: 0.149 / Χ2: 0.961 / Net I/σ(I): 4.5 / Num. measured all: 49420
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3-3.115.50.4947370.9060.2250.5450.98895.2
3.11-3.235.90.3997790.9380.1760.4370.94698.6
3.23-3.386.40.3277870.9670.1390.3560.95399.9
3.38-3.566.50.2287810.9890.0970.2480.997100
3.56-3.786.50.1927980.9870.0820.2090.999100
3.78-4.076.10.1567880.990.0680.171.0399.9
4.07-4.486.40.1118120.9930.0470.1210.992100
4.48-5.136.50.0938120.9950.0390.1020.95599.9
5.13-6.4660.0978250.9920.0430.1060.905100
6.46-505.90.0768830.9940.0340.0830.8599.8

-
Processing

Software
NameVersionClassification
SCALEPACKdata scaling
REFMAC5.8.0257refinement
PDB_EXTRACT3.25data extraction
Cootmodel building
PHASERphasing
HKL-3000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1QZG, 4HIK
Resolution: 3→46.44 Å / Cor.coef. Fo:Fc: 0.874 / Cor.coef. Fo:Fc free: 0.833 / SU B: 61.272 / SU ML: 0.487 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.598 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2976 372 5 %RANDOM
Rwork0.2674 ---
obs0.2689 7049 92.17 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 173.72 Å2 / Biso mean: 71.424 Å2 / Biso min: 22.42 Å2
Baniso -1Baniso -2Baniso -3
1-1.26 Å20 Å20 Å2
2--0.06 Å20 Å2
3----1.32 Å2
Refinement stepCycle: final / Resolution: 3→46.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2522 377 0 0 2899
Num. residues----323
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.0123007
X-RAY DIFFRACTIONr_angle_refined_deg1.2821.5644148
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.1445303
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.5822.276145
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.46815466
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.3161517
X-RAY DIFFRACTIONr_chiral_restr0.0940.2383
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022168
LS refinement shellResolution: 3→3.078 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.31 15 -
Rwork0.298 362 -
all-377 -
obs--65.79 %
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)
12.7044-1.79070.00451.41190.09140.1346-0.1059-0.2452-0.28590.05670.16950.1421-0.0336-0.0815-0.06360.01730.03140.00080.09740.0770.2210.1656-6.1753-17.4481
210.8447-2.77061.14151.24280.39171.4226-0.60950.1922-0.22840.11660.09310.253-0.0483-0.06020.51640.29240.0280.10080.2333-0.10920.287115.2374-7.7104-33.7371
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A8 - 337
2X-RAY DIFFRACTION2B1 - 18

+
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