[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

TitleCryo-EM structures of CCHFV polymerase reveal a stepwise initiation stabilization pathway and a dual-site inhibition mechanism.
Journal, issue, pagesCell Rep, Vol. 45, Issue 9, Page 117945, Year 2026
Publish dateSep 3, 2026
AuthorsKankan Yang / Haiqiang Wu / Xunbi Liu / Zuxing Liang / Junwei Zou / Yong Wang / Jun Ma /
PubMed AbstractCrimean-Congo hemorrhagic fever virus (CCHFV) is a high-priority pathogen with high case-fatality rates, yet approved therapeutics remain unavailable. The CCHFV L segment encodes a ∼450-kDa RNA- ...Crimean-Congo hemorrhagic fever virus (CCHFV) is a high-priority pathogen with high case-fatality rates, yet approved therapeutics remain unavailable. The CCHFV L segment encodes a ∼450-kDa RNA-dependent RNA polymerase (L protein) orchestrating viral replication, but its structural mechanisms remain elusive. Here, we present high-resolution cryo-EM structures of the CCHFV L protein in apo, 5' vRNA-bound, 5'/3' promoter-bound, and inhibitor-bound states. The catalytic core exhibits the canonical architecture of the Bunyavirales order, featuring conserved motifs and coordinated promoter recognition via a 5' vRNA "hook" and a secondary 3' vRNA-binding site. Using suramin as a probe, we identified a dual-site mechanism of polymerase inhibition. Suramin competitively occludes the 5' vRNA-binding pocket through electrostatic mimicry of the RNA backbone and concurrently traps a distal linker-fingers interface, restricting the conformational dynamics required for catalysis. Collectively, these findings provide structural insights into CCHFV polymerase regulation and inhibition.
External linksCell Rep / PubMed:42696455
MethodsEM (single particle)
Resolution2.5 - 3.03 Å
Structure data

EMDB-68655, PDB-22te:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in apo state
Method: EM (single particle) / Resolution: 2.59 Å

EMDB-68657, PDB-22th:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in complex with suramin
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-68663, PDB-22tr:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in complex with 5' vRNA promotor
Method: EM (single particle) / Resolution: 2.75 Å

EMDB-80706, PDB-26jz:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in complex with 5'/3' vRNA dual-promotor
Method: EM (single particle) / Resolution: 2.65 Å

EMDB-80707, PDB-26ka:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in complex with the 5' vRNA promotor from the 5'/3' vRNA dual-promoter dataset
Method: EM (single particle) / Resolution: 3.03 Å

EMDB-80708, PDB-26kb:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in the apo3 state from the 5'/3' vRNA dual-promoter dataset
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-80710, PDB-26kd:
Cryo-EM structure of Crimean-Congo hemorrhagic fever virus RNA polymerase in the apo2 state from the 5'/3' vRNA dual-promoter dataset
Method: EM (single particle) / Resolution: 2.64 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-SVR:
8,8'-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFON / medication*YM

Source
  • orthonairovirus haemorrhagiae
  • crimean-congo hemorrhagic fever virus strain ibar10200
  • Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)
KeywordsRNA BINDING PROTEIN / Polymerase / RNA BINDING PROTEIN/RNA / RNA BINDING PROTEIN-RNA complex

+
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