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Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex

by single particle reconstruction, at 11.1 A resolution

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#1: Depositted structure unit, Made by Jmol

#2: Superimposing with simplified surface model of EM map, EMDB-1915, Made by Jmol

#3: Superimposing with simplified surface model of EM map, EMDB-1916, Made by Jmol

#4: Superimposing with EM 3D map: EMDB-1915, Made by UCSF CHIMERA

#5: Superimposing with EM 3D map: EMDB-1916, Made by UCSF CHIMERA

Entry
Summary
Database / IDPORTEIN DATA BANK (PDB) / 3j0d
TitleModels for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex
DescriptorPROTEIN/RNA Complex
KeywordsTRANSLATION, ribosome, ribosome recycling factor
AuthorsYokoyama, T., Shaikh, T.R., Iwakura, N., Kaji, H., Kaji, A., Agrawal, R.K.
DateDeposition: 2011-06-29, Release: 2012-04-25
PDBj Mine pagesSummary, Structural Details, Experimental Details, Functional Details
Other databasesRCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST
Sequence detailsRIBOSOMAL RNA IS ONLY PARTIALLY MODELED IN THIS ENTRY: CHAINS A-F ARE PARTS OF THE 23S RIBOSOMAL RNA AND CHAINS H AND h ARE PARTS OF THE 16S RIBOSOMAL RNA.
Structure Visualization
MoviesMovie Page

#1: Depositted structure unit, Made by Jmol

#2: Superimposing with simplified surface model of EM map, EMDB-1915, Made by Jmol

#3: Superimposing with simplified surface model of EM map, EMDB-1916, Made by Jmol

#4: Superimposing with EM 3D map: EMDB-1915, Made by UCSF CHIMERA

#5: Superimposing with EM 3D map: EMDB-1916, Made by UCSF CHIMERA

Structure viewersYorodumi, jV4, Jmol, Biological unit (Images, jV)
Related Structure Data
Related Entries

EMDB-1915

CiteFit

EMDB-1916

CiteFit

Cite: data citing same article

Fit: target map of fitting

Similar strucutres (beta)
List of similar structure data about Omokage system
Article
Citation - primary
ArticleEMBO J., Vol. 31, Issue 7, Page 1836-46, Year 2012
TitleStructural insights into initial and intermediate steps of the ribosome-recycling process.
AuthorsTakeshi Yokoyama, Tanvir R Shaikh, Nobuhiro Iwakura, Hideko Kaji, Akira Kaji, Rajendra K Agrawal
Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
KeywordsCryoelectron Microscopy, Escherichia coli (metabolism), Escherichia coli Proteins (metabolism), L11 protein, E coli, Peptide Elongation Factor G (metabolism), Protein Binding, Protein Conformation, RNA, Ribosomal (metabolism), Ribosomal Proteins (metabolism), Ribosomes (metabolism), ribosome releasing factor
LinksDOI: 10.1038/emboj.2012.22, PubMed: 22388519, PMC: PMC3321202
Components
ID 1 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelices 43 and 44
Formula weight16114.751 Da
Number of molecules1
ID1
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli

LinksGenBank: U00096.2, Sequence view
ID 2 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelix 69
Formula weight6994.250 Da
Number of molecules1
ID2
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 3 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelix 71
Formula weight5459.323 Da
Number of molecules1
ID3
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 4 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelix 80
Formula weight4228.593 Da
Number of molecules1
ID4
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 5 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelix 93
Formula weight6117.740 Da
Number of molecules1
ID5
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 6 : ribosomal 23S RNA
Image
Descriptionribosomal 23S RNA
Typepolyribonucleotide
Fragmenthelix 95
Formula weight6155.794 Da
Number of molecules1
ID6
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 7 : 50S ribosomal protein L11
Image
Description50S ribosomal protein L11
Typepolypeptide(L)
Formula weight14763.286 Da
Number of molecules1
ID7
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksUniProt: P0A7J7, Sequence view
ID 8 : ribosomal 16S RNA
Image
Descriptionribosomal 16S RNA
Typepolyribonucleotide
Fragmenthelix 44 strand 1
Formula weight5787.546 Da
Number of molecules1
ID8
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 9 : ribosomal 16S RNA
Image
Descriptionribosomal 16S RNA
Typepolypeptide(L)
Fragmenthelix 44 strand 2
Formula weight6173.764 Da
Number of molecules1
ID9
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksGenBank: U00096.2, Sequence view
ID 10 : 30S ribosomal protein S12
Image
Description30S ribosomal protein S12
Typepolypeptide(L)
Formula weight13637.070 Da
Number of molecules1
ID10
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:562
Organism scientific: Escherichia coli
LinksUniProt: P0A7S3, Sequence view
ID 11 : RRF, Ribosome-releasing factor
Image
DescriptionRibosome-recycling factor
Typepolyribonucleotide
Formula weight21029.262 Da
Number of molecules1
ID11
SourceMethod: Isolated from a natural source
NCBI taxonomy: ID:274
Organism scientific: Thermus thermophilus
LinksUniProt: Q9WX76, Sequence view
Sample
Assembly
Aggregation statePARTICLE
DetailsPOTC-TTRRF
NameE. COLI POST TERMINATION COMPLEX
Buffer
NameBUFFER R
Experiment
Reconstruction methodSINGLE PARTICLE
Specimen typeVITREOUS ICE (CRYO EM)
Sample preparation
pH7.50
Sample concentration0.08 mg/ml
Sample support
DetailsQUANTIFOIL HOLEY CARBON FILM G
Vitrification
DetailsVITROBOT
Experiment
MethodELECTRON MICROSCOPY
Electron Microscopy
Imaging
MicroscopeModel: TECNAI F20
Date2010-12-23
Electron gun
Electron sourceFIELD EMISSION GUN
Accelerating voltage200 kV
Lens
MagnificationCalibrated: 50310 X, Nominal: 50000 X
Nominal defocusMax: 4300.00 nm, Min: 400.00 nm
Specimen holder
Tilt angleMin: 0.00 degrees, Max: 0.00 degrees
Temperature93.00 Kelvin
Detector
TypeKODAK S0163 FILM
Processing
2D projection selection
Number of particles153927
Software nameSPIDER
Single particle entity
Symmetry typeASYMMETRIC
3D reconstruction
CTF correction methodCTF CORRECTION OF 3D MAPS BY WIENER FILTRATION
Method3D PROJECTION MATCHING
Nominal pixel size2.78 A/pix
Resolution11.1 A
3D fitting
Refinement ProtocolFLEXIBLE FITTING (MDFF)
3D fitting list
3D fitting id1
PDB entry IDPDB ID 2AVY, 2AW4, 1EH1
Refine hist
Cycle idLAST
Refine idELECTRON MICROSCOPY
Total atoms7260
Nucleic acid atoms3796
Protein atoms3464
Download
PDB format
Allpdb3j0d.ent.gz
pdb3j0d.ent (uncompressed file)
Header onlypdb3j0d.ent.gz
mmCIF format
mmCIF3j0d.cif.gz
XML format
All3j0d.xml.gz
No-atom3j0d-noatom.xml.gz
Ext-atom3j0d-extatom.xml.gz
Movie files
movie #1
.mp4 (H.264/MPEG-4 AVC format), 2.5 MB
.webm (WebM/VP8 format), 3.4 MB
movie #2
.mp4 (H.264/MPEG-4 AVC format), 3.6 MB
.webm (WebM/VP8 format), 5.2 MB
movie #3
.mp4 (H.264/MPEG-4 AVC format), 2.7 MB
.webm (WebM/VP8 format), 3.7 MB
movie #4
.mp4 (H.264/MPEG-4 AVC format), 3.3 MB
.webm (WebM/VP8 format), 4.3 MB
movie #5
.mp4 (H.264/MPEG-4 AVC format), 3.6 MB
.webm (WebM/VP8 format), 5 MB