[English] 日本語
Yorodumi
- EMDB-30626: Mouse Toll-like receptor 3 ectodomain in complex with lncRNA Rmrp... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-30626
TitleMouse Toll-like receptor 3 ectodomain in complex with lncRNA Rmrp in lapped form
Map data
Sample
  • Complex: Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C-domain of lncRNA Rmrp
    • Complex: Toll-like receptor 3
      • Protein or peptide: Toll-like receptor 3
    • Complex: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA
      • RNA: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA
Keywordscomplex / innate immune system / RNA BINDING PROTEIN / RNA BINDING PROTEIN-RNA complex
Function / homology
Function and homology information


type III interferon production / positive regulation of type III interferon production / response to dsRNA / regulation of dendritic cell cytokine production / inflammatory response to wounding / toll-like receptor 3 signaling pathway / necroptotic signaling pathway / positive regulation of cytokine production involved in inflammatory response / positive regulation of macrophage cytokine production / pattern recognition receptor activity ...type III interferon production / positive regulation of type III interferon production / response to dsRNA / regulation of dendritic cell cytokine production / inflammatory response to wounding / toll-like receptor 3 signaling pathway / necroptotic signaling pathway / positive regulation of cytokine production involved in inflammatory response / positive regulation of macrophage cytokine production / pattern recognition receptor activity / toll-like receptor signaling pathway / cellular response to exogenous dsRNA / response to exogenous dsRNA / positive regulation of interferon-alpha production / positive regulation of type I interferon production / cellular response to interferon-beta / positive regulation of chemokine production / JNK cascade / extrinsic apoptotic signaling pathway / positive regulation of interleukin-12 production / positive regulation of interferon-beta production / positive regulation of interleukin-8 production / positive regulation of JNK cascade / microglial cell activation / response to virus / cellular response to virus / cellular response to type II interferon / defense response / positive regulation of interleukin-6 production / cellular response to mechanical stimulus / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of type II interferon production / positive regulation of angiogenesis / male gonad development / positive regulation of tumor necrosis factor production / MAPK cascade / transmembrane signaling receptor activity / double-stranded RNA binding / cellular response to xenobiotic stimulus / signaling receptor activity / defense response to virus / positive regulation of canonical NF-kappaB signal transduction / early endosome / endosome membrane / inflammatory response / positive regulation of apoptotic process / innate immune response / endoplasmic reticulum membrane / cell surface / positive regulation of transcription by RNA polymerase II / identical protein binding / plasma membrane
Similarity search - Function
Toll-like receptor 3 trans-membrane domain / Toll-like receptor 3 trans-membrane domain / Toll-like receptor / TIR domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Leucine Rich Repeat / Toll - interleukin 1 - resistance / TIR domain profile. / Leucine-rich repeat, SDS22-like subfamily ...Toll-like receptor 3 trans-membrane domain / Toll-like receptor 3 trans-membrane domain / Toll-like receptor / TIR domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Leucine Rich Repeat / Toll - interleukin 1 - resistance / TIR domain profile. / Leucine-rich repeat, SDS22-like subfamily / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily
Similarity search - Domain/homology
Toll-like receptor 3
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.64 Å
AuthorsLi B / Cao X
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81788101 China
CitationJournal: To Be Published
Title: Endosomal lncRNA Rmrp is required for TLR3 innate sensing by engaging TLR3 dimerization
Authors: Zhang S / Li B / Cao X
History
DepositionOct 18, 2020-
Header (metadata) releaseOct 20, 2021-
Map releaseOct 20, 2021-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.33
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.33
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7das
  • Surface level: 0.33
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_30626.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 384 pix.
= 314.88 Å
0.82 Å/pix.
x 384 pix.
= 314.88 Å
0.82 Å/pix.
x 384 pix.
= 314.88 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density
Contour LevelBy AUTHOR: 0.29 / Movie #1: 0.33
Minimum - Maximum-0.6003012 - 1.3100822
Average (Standard dev.)0.0022979598 (±0.036890317)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 314.88 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.820.820.82
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z314.880314.880314.880
α/β/γ90.00090.00090.000
start NX/NY/NZ-250-250-250
NX/NY/NZ500500500
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-0.6001.3100.002

-
Supplemental data

-
Sample components

-
Entire : Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C...

EntireName: Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C-domain of lncRNA Rmrp
Components
  • Complex: Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C-domain of lncRNA Rmrp
    • Complex: Toll-like receptor 3
      • Protein or peptide: Toll-like receptor 3
    • Complex: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA
      • RNA: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA

-
Supramolecule #1: Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C...

SupramoleculeName: Cryo-EM structure of mouse Toll-like receptor 3 ectodomain with C-domain of lncRNA Rmrp
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Molecular weightTheoretical: 230 KDa

-
Supramolecule #2: Toll-like receptor 3

SupramoleculeName: Toll-like receptor 3 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)

-
Supramolecule #3: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA

SupramoleculeName: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA
type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Mus musculus (house mouse)

-
Macromolecule #1: Toll-like receptor 3

MacromoleculeName: Toll-like receptor 3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 78.101648 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: HHHHHHENLY FQSQCTVRYN VADCSHLKLT HIPDDLPSNI TVLNLTHNQL RRLPPTNFTR YSQLAILDAG FNSISKLEPE LCQILPLLK VLNLQHNELS QISDQTFVFC TNLTELDLMS NSIHKIKSNP FKNQKNLIKL DLSHNGLSST KLGTGVQLEN L QELLLAKN ...String:
HHHHHHENLY FQSQCTVRYN VADCSHLKLT HIPDDLPSNI TVLNLTHNQL RRLPPTNFTR YSQLAILDAG FNSISKLEPE LCQILPLLK VLNLQHNELS QISDQTFVFC TNLTELDLMS NSIHKIKSNP FKNQKNLIKL DLSHNGLSST KLGTGVQLEN L QELLLAKN KILALRSEEL EFLGNSSLRK LDLSSNPLKE FSPGCFQTIG KLFALLLNNA QLNPHLTEKL CWELSNTSIQ NL SLANNQL LATSESTFSG LKWTNLTQLD LSYNNLHDVG NGSFSYLPSL RYLSLEYNNI QRLSPRSFYG LSNLRYLSLK RAF TKQSVS LASHPNIDDF SFQWLKYLEY LNMDDNNIPS TKSNTFTGLV SLKYLSLSKT FTSLQTLTNE TFVSLAHSPL LTLN LTKNH ISKIANGTFS WLGQLRILDL GLNEIEQKLS GQEWRGLRNI FEIYLSYNKY LQLSTSSFAL VPSLQRLMLR RVALK NVDI SPSPFRPLRN LTILDLSNNN IANINEDLLE GLENLEILDF QHNNLARLWK RANPGGPVNF LKGLSHLHIL NLESNG LDE IPVGVFKNLF ELKSINLGLN NLNKLEPFIF DDQTSLRSLN LQKNLITSVE KDVFGPPFQN LNSLDMRFNP FDCTCES IS WFVNWINQTH TNISELSTHY LCNTPHHYYG FPLKLFDTSS CK

UniProtKB: Toll-like receptor 3

-
Macromolecule #2: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA

MacromoleculeName: RNA component of mitochondrial RNAase P (Rmrp), RNase MRP RNA
type: rna / ID: 2 / Number of copies: 1
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 48.12452 KDa
SequenceString:
GCUCGCUCUG AAGGCCUGUU UCCUAGGCUA CAUACGAGGG ACAUGUUCCU UAUCCUUUCG CCUAGGGGAA AGUCCCCGGA AGCUCACAU AGUGACGCAG GCAGUGCGAC CUGGCUCGCA CCAACCACAC GGGGCUCAUU CUCAGCGCGG C

GENBANK: GENBANK: NR_001460.1, GENBANK: NR_001460.1

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration1.0 mg/mL
BufferpH: 6
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 25 sec. / Pretreatment - Atmosphere: OTHER / Pretreatment - Pressure: 101.325 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV
DetailsThis sample was mono disperse.

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMin: 78.5 K / Max: 78.5 K
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 40 eV
DetailsPreliminary grid screening was preformed manually.
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Number grids imaged: 2 / Number real images: 10617 / Average exposure time: 5.0 sec. / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 2.0 µm / Calibrated defocus min: 1.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 165000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

DetailsThe selected images were normalized.
Particle selectionNumber selected: 2545278
Startup modelType of model: NONE / Details: The startup models were generated automatically.
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.64 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2.9.1) / Number images used: 99902
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2.9.1)
Details: The initial angle assignment was generated by Ab-initio reconstruction.
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2.9.1)
Final 3D classificationNumber classes: 5 / Software - Name: cryoSPARC (ver. 2.9.1)

-
Atomic model buiding 1

Initial modelPDB ID:

Chain - Chain ID: A / Chain - Residue range: 27-697 / Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementProtocol: RIGID BODY FIT / Overall B value: 97.5 / Target criteria: correlation coefficient
Output model

PDB-7das:
Mouse Toll-like receptor 3 ectodomain in complex with lncRNA Rmrp in lapped form

+
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