[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 of the bacterial defense-associated sirtuin system.
Journal, issue, pagesCommun Biol, Vol. 8, Issue 1, Page 297, Year 2025
Publish dateFeb 24, 2025
AuthorsKaixiang Zhu / Kun Shang / Linyue Wang / Xia Yu / Lei Hua / Weihe Zhang / Bo Qin / Jia Wang / Xiaopan Gao / Hongtao Zhu / Sheng Cui /
PubMed AbstractThe NADase activity of the defense-associated sirtuins (DSRs) is activated by the phage tail tube protein (TTP). Herein, we report cryo-EM structures of a free-state Bacillus subtilis DSR2 tetramer ...The NADase activity of the defense-associated sirtuins (DSRs) is activated by the phage tail tube protein (TTP). Herein, we report cryo-EM structures of a free-state Bacillus subtilis DSR2 tetramer and a fragment of the tetramer, a phage SPR tail tube, and two DSR2-TTP complexes. DSR2 contains an N-terminal SIR2 domain, a middle domain (MID) and a C-terminal domain (CTD). The DSR2 CTD harbors the α-solenoid tandem-repeats like the HEAT-repeat proteins. DSR2 assembles into a tetramer with four SIR2 clustered at the center, and two intertwined MID-CTD chains flank the SIR2 core. SPR TTPs self-assemble into a tube-like complex. Upon DSR2 binding, the D1 domain of SPR TTP is captured between the HEAT-repeats domains of DSR2, which conflicts with TTPs self-assembly. Binding of TTPs induces conformational changes in DSR2 tetramer, resulting in increase of the NAD pocket volume in SIR2, thus activates the NADase activity and leads to cellular NAD depletion.
External linksCommun Biol / PubMed:39994439 / PubMed Central
MethodsEM (single particle)
Resolution3.29 - 4.66 Å
Structure data

EMDB-39233, PDB-8yg1:
The Dimer Structure of DSR2 alone
Method: EM (single particle) / Resolution: 3.74 Å

EMDB-39240, PDB-8yga:
The tetramer Structure of DSR2 alone
Method: EM (single particle) / Resolution: 4.53 Å

EMDB-39243, PDB-8ygc:
The Dimer Structure of DSR2-SPR
Method: EM (single particle) / Resolution: 4.03 Å

EMDB-39246, PDB-8ygf:
The tetramer Structure of SPR-DSR2 complex
Method: EM (single particle) / Resolution: 4.66 Å

EMDB-39254, PDB-8ygk:
The dimer Structure of SPR-DSR2(CTD) complex
Method: EM (single particle) / Resolution: 3.78 Å

EMDB-39256, PDB-8ygm:
The cryo-EM Structure of SPR
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-39257, PDB-8ygn:
The Dimer Structure of DSR2-SPR with NAD
Method: EM (single particle) / Resolution: 4.27 Å

EMDB-39258, PDB-8ygo:
The complex by DSR2-CTD-SPR with NAD
Method: EM (single particle) / Resolution: 3.29 Å

EMDB-39259, PDB-8ygp:
The tetramer Structure of DSR2-SPR with NAD
Method: EM (single particle) / Resolution: 4.4 Å

Source
  • bacillus subtilis a29 (bacteria)
KeywordsHYDROLASE / SIR2 / NADase / dimer / SPR / DSR2-CTD / tetramer

+
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