[English] 日本語
Yorodumi
- EMDB-50055: Cryo-EM structure of SAVED-Lon protease CCaCalpL filament bound to cA4 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-50055
TitleCryo-EM structure of SAVED-Lon protease CCaCalpL filament bound to cA4
Map data
Sample
  • Complex: Filament fragment of cA4 bound CCaCalpL
    • Complex: CCaCalpL
      • Protein or peptide: SMODS-associated and fused to various effectors domain-containing protein
    • Complex: cA4
      • RNA: cA4
KeywordsLON PROTEASE / SAVED DOMAIN / CRISPR / HYDROLASE
Function / homologySMODS-associated and fused to various effectors / SMODS-associated and fused to various effectors sensor domain / SMODS-associated and fused to various effectors domain-containing protein
Function and homology information
Biological speciesCandidatus Cloacimonas acidaminovorans (bacteria) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.97 Å
AuthorsTamulaitiene G / Sasnauskas G / Smalakyte D / Tamulaitis G
Funding supportLithuania, 1 items
OrganizationGrant numberCountry
Research Council of LithuaniaS-MIP-22-9Lithuania
CitationJournal: To Be Published
Title: Cryo-EM structure of SAVED-Lon protease CCaCalpL filament bound to cA4
Authors: Smalakyte D / Ruksenaite A / Sasnauskas G / Tamulaitiene G / Tamulaitis G
History
DepositionApr 9, 2024-
Header (metadata) releaseOct 2, 2024-
Map releaseOct 2, 2024-
UpdateOct 2, 2024-
Current statusOct 2, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_50055.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
1.1 Å/pix.
x 240 pix.
= 264. Å
1.1 Å/pix.
x 240 pix.
= 264. Å
1.1 Å/pix.
x 240 pix.
= 264. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density
Contour LevelBy AUTHOR: 7.0
Minimum - Maximum-22.984999999999999 - 43.563408000000003
Average (Standard dev.)0.000000000003838 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 264.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_50055_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Additional map: #1

Fileemd_50055_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_50055_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_50055_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Filament fragment of cA4 bound CCaCalpL

EntireName: Filament fragment of cA4 bound CCaCalpL
Components
  • Complex: Filament fragment of cA4 bound CCaCalpL
    • Complex: CCaCalpL
      • Protein or peptide: SMODS-associated and fused to various effectors domain-containing protein
    • Complex: cA4
      • RNA: cA4

-
Supramolecule #1: Filament fragment of cA4 bound CCaCalpL

SupramoleculeName: Filament fragment of cA4 bound CCaCalpL / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

-
Supramolecule #2: CCaCalpL

SupramoleculeName: CCaCalpL / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Candidatus Cloacimonas acidaminovorans (bacteria)

-
Supramolecule #3: cA4

SupramoleculeName: cA4 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: synthetic construct (others)

-
Macromolecule #1: SMODS-associated and fused to various effectors domain-containing...

MacromoleculeName: SMODS-associated and fused to various effectors domain-containing protein
type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Candidatus Cloacimonas acidaminovorans (bacteria) / Strain: Evry
Molecular weightTheoretical: 63.294172 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MGGSHHHHHH GMASWSHPQF EKGGHHHHHH GGSGENLYFQ GGSGPKFNET ADKYLKSGSA EAELIILQYI QQDRVSEDDE EWVYNLLEK ANNPYIKLNA LLWLSAKRKY LTQLSKLWGI SENELKSLSQ QQPKIGLFPA VDSRKNAFLA KVFVYKLKSE E PIALAILG ...String:
MGGSHHHHHH GMASWSHPQF EKGGHHHHHH GGSGENLYFQ GGSGPKFNET ADKYLKSGSA EAELIILQYI QQDRVSEDDE EWVYNLLEK ANNPYIKLNA LLWLSAKRKY LTQLSKLWGI SENELKSLSQ QQPKIGLFPA VDSRKNAFLA KVFVYKLKSE E PIALAILG DKIENFSYLA QLGKQNCLIG FNKNIQGNSW QLAVLATLLV KDEKIISKIA YSGIVLPSGE IITAEEIEYK KR CCQNLVH RIKKIEQLDA WLNTETIPLP VIQYQGEENE LKRWQKAMEQ KVQEKFSWFS YELLEDFYGI TNSDLAIFGN GIL PFEANA WQKLLQEQVK DKFKLLEDKV MPKKVLWFYA GQISTLQLGI GALFGFKRAV SILQMEFSNT TYHEVFILYG KENA RQLKN VSVKKEDYQY IQSELLINEP HKNELGFIIY LGSHNPIGEA KAYCQKQLQI NNFLIIQARE NQGVMETSQN WLPYL QEIN SALNTARQEY HWERIHLFQT APTALCMALG IAVGHFLPVD VYHYQFNAEE PKYRCVFSLD KMLNL

UniProtKB: SMODS-associated and fused to various effectors domain-containing protein

-
Macromolecule #2: cA4

MacromoleculeName: cA4 / type: rna / ID: 2 / Number of copies: 1
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 1.271866 KDa
SequenceString:
AAAA

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

-
Sample preparation

Concentration1 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 30.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 92000

+
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.97 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v4.4.1) / Number images used: 124470
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

+
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