[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

TitleMolecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 31, Page 18711-18718, Year 2020
Publish dateAug 4, 2020
AuthorsYingzi Cui / Ruchao Peng / Hao Song / Zhou Tong / Xiao Qu / Sheng Liu / Xin Zhao / Yan Chai / Peiyi Wang / George F Gao / Jianxun Qi /
PubMed AbstractKREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. ...KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection.
External linksProc Natl Acad Sci U S A / PubMed:32690697 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.6 Å
Structure data

EMDB-30253, PDB-7bzn:
Cryo-EM structure of mature Coxsackievirus A10 at pH 7.4
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-30254, PDB-7bzo:
Cryo-EM structure of mature Coxsackievirus A10 at pH 5.5
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30259, PDB-7bzt:
Cryo-EM structure of mature Coxsackievirus A10 in complex with KRM1 at pH 7.4
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-30260, PDB-7bzu:
Cryo-EM structure of mature Coxsackievirus A10 in complex with KRM1 at pH 5.5
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-30287, PDB-7c4t:
Cryo-EM structure of A particle Coxsackievirus A10 at pH 7.4
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-30290, PDB-7c4w:
Cryo-EM structure of A particle Coxsackievirus A10 at pH 5.5
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-30291, PDB-7c4y:
Cryo-EM structure of empty Coxsackievirus A10 at pH 7.4
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-30292, PDB-7c4z:
Cryo-EM structure of empty Coxsackievirus A10 at pH 5.5
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • coxsackievirus a10
  • homo sapiens (human)
KeywordsVIRUS / Picornavirus / Coxsackievirus A10 / pH 7.4 / mature particle / pH 5.5 / KRM1 / complex / A particle / empty particle

+
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