[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

TitleGenome expansion by a CRISPR trimmer-integrase.
Journal, issue, pagesNature, Vol. 618, Issue 7966, Page 855-861, Year 2023
Publish dateJun 14, 2023
AuthorsJoy Y Wang / Owen T Tuck / Petr Skopintsev / Katarzyna M Soczek / Gary Li / Basem Al-Shayeb / Julia Zhou / Jennifer A Doudna /
PubMed AbstractCRISPR-Cas adaptive immune systems capture DNA fragments from invading mobile genetic elements and integrate them into the host genome to provide a template for RNA-guided immunity. CRISPR systems ...CRISPR-Cas adaptive immune systems capture DNA fragments from invading mobile genetic elements and integrate them into the host genome to provide a template for RNA-guided immunity. CRISPR systems maintain genome integrity and avoid autoimmunity by distinguishing between self and non-self, a process for which the CRISPR/Cas1-Cas2 integrase is necessary but not sufficient. In some microorganisms, the Cas4 endonuclease assists CRISPR adaptation, but many CRISPR-Cas systems lack Cas4. Here we show here that an elegant alternative pathway in a type I-E system uses an internal DnaQ-like exonuclease (DEDDh) to select and process DNA for integration using the protospacer adjacent motif (PAM). The natural Cas1-Cas2/exonuclease fusion (trimmer-integrase) catalyses coordinated DNA capture, trimming and integration. Five cryo-electron microscopy structures of the CRISPR trimmer-integrase, visualized both before and during DNA integration, show how asymmetric processing generates size-defined, PAM-containing substrates. Before genome integration, the PAM sequence is released by Cas1 and cleaved by the exonuclease, marking inserted DNA as self and preventing aberrant CRISPR targeting of the host. Together, these data support a model in which CRISPR systems lacking Cas4 use fused or recruited exonucleases for faithful acquisition of new CRISPR immune sequences.
External linksNature / PubMed:37316664 / PubMed Central
MethodsEM (single particle)
Resolution2.91 - 4.1 Å
Structure data

EMDB-29561, PDB-8fy9:
Cryo-EM structure of Cas1:Cas2-DEDDh:PAM-deficient prespacer complex
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-29562, PDB-8fya:
Cryo-EM structure of Cas1:Cas2-DEDDh:PAM-containing prespacer complex
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-29563, PDB-8fyb:
Cryo-EM structure of Cas1:Cas2-DEDDh:half-site integration complex
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-29564, PDB-8fyc:
Cryo-EM structure of Cas1:Cas2-DEDDh:half-site integration complex linear CRISPR repeat conformation
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-29565, PDB-8fyd:
Cryo-EM structure of Cas1:Cas2-DEDDh:half-site integration complex bent CRISPR repeat conformation
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • megasphaera (bacteria)
KeywordsDNA BINDING PROTEIN/DNA / CRISPR / integrase / CRISPR adaptation module / PAM / prespacer / exonuclease / DNA binding protein-DNA complex / enzyme / ribonucleoprotein

+
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://pdbjlvh1.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