[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleActivation mechanism of a short argonaute-TIR prokaryotic immune system.
Journal, issue, pagesSci Adv, Vol. 9, Issue 29, Page eadh9002, Year 2023
Publish dateJul 21, 2023
AuthorsDongchun Ni / Xuhang Lu / Henning Stahlberg / Babatunde Ekundayo /
PubMed AbstractShort prokaryotic argonaute (pAgo) and toll/interleukin-1 receptor/resistance protein (TIR)-analog of PAZ (APAZ) form a heterodimeric SPARTA complex that provides immunity to its prokaryotic host ...Short prokaryotic argonaute (pAgo) and toll/interleukin-1 receptor/resistance protein (TIR)-analog of PAZ (APAZ) form a heterodimeric SPARTA complex that provides immunity to its prokaryotic host through an abortive infection mechanism. Monomeric SPARTA senses foreign RNA/DNA duplexes to assemble an active tetramer resulting in cell death by nicotinamide adenine dinucleotide (oxidized form) (NAD) depletion via an unknown mechanism. We report nine structures of SPARTA in different functional states at a resolution range of 4.2 to 2.9 angstroms, revealing its activation mechanism. Inactive SPARTA monomers bind to RNA/DNA duplexes to form symmetric dimers mediated by the association of Ago subunits. The initiation of tetramer assembly induces flexibility of the TIR domains enabling a symmetry-breaking rotational movement of a TIR domain in the dimer units which facilitates the TIR oligomerization, resulting in the formation of the substrate binding pocket and the activation of the SPARTA complex's NADase activity. Our findings provide detailed structural and mechanistic insights into activating a short argonaute defense system.
External linksSci Adv / PubMed:37467330 / PubMed Central
MethodsEM (single particle)
Resolution2.91 - 4.85 Å
Structure data

EMDB-17299, PDB-8oz6:
cryoEM structure of SPARTA complex ligand-free
Method: EM (single particle) / Resolution: 3.97 Å

EMDB-17300: Duplex-bound tetramer high-resolution (EMDB-xxxx) SPARTA complex
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-17301: Dimer-1 SPARTA complex
Method: EM (single particle) / Resolution: 3.31 Å

EMDB-17302: Dimer-2 SPARTA complex
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-17303: monomer-duplex bound
Method: EM (single particle) / Resolution: 4.85 Å

EMDB-17304, PDB-8ozc:
cryoEM structure of SPARTA complex heterodimer apo
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-17305, PDB-8ozd:
cryoEM structure of SPARTA complex dimer-3
Method: EM (single particle) / Resolution: 3.89 Å

EMDB-17306, PDB-8oze:
cryoEM structure of SPARTA complex dimer high resolution
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-17307, PDB-8ozf:
cryoEM structure of SPARTA complex Tetramer Post-NAD cleavage-2
Method: EM (single particle) / Resolution: 3.73 Å

EMDB-17308, PDB-8ozg:
cryoEM structure of SPARTA complex Tetramer Post-NAD cleavage-1
Method: EM (single particle) / Resolution: 3.37 Å

EMDB-17310, PDB-8ozi:
cryoEM structure of SPARTA complex pre-NAD cleavage
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-AR6:
[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL

ChemComp-MG:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide

Source
  • maribacter polysiphoniae (bacteria)
KeywordsANTIVIRAL PROTEIN / SPARTA / TIR / prokaryotic argonaute / DNA BINDING PROTEIN / IMMUNE SYSTEM

+
About Yorodumi Papers

-
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 Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more