[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

TitleStructural insights into the functional mechanism of the ubiquitin ligase E6AP.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3531, Year 2024
Publish dateApr 26, 2024
AuthorsZhen Wang / Fengying Fan / Zhihai Li / Fei Ye / Qingxia Wang / Rongchao Gao / Jiaxuan Qiu / Yixin Lv / Min Lin / Wenwen Xu / Cheng Luo / Xuekui Yu /
PubMed AbstractE6AP dysfunction is associated with Angelman syndrome and Autism spectrum disorder. Additionally, the host E6AP is hijacked by the high-risk HPV E6 to aberrantly ubiquitinate the tumor suppressor ...E6AP dysfunction is associated with Angelman syndrome and Autism spectrum disorder. Additionally, the host E6AP is hijacked by the high-risk HPV E6 to aberrantly ubiquitinate the tumor suppressor p53, which is linked with development of multiple types of cancer, including most cervical cancers. Here we show that E6AP and the E6AP/E6 complex exist, respectively, as a monomer and a dimer of the E6AP/E6 protomer. The short α1-helix of E6AP transforms into a longer helical structure when in complex with E6. The extended α1-helices of the dimer intersect symmetrically and contribute to the dimerization. The two protomers sway around the crossed region of the two α1-helices to promote the attachment and detachment of substrates to the catalytic C-lobe of E6AP, thus facilitating ubiquitin transfer. These findings, complemented by mutagenesis analysis, suggest that the α1-helix, through conformational transformations, controls the transition between the inactive monomer and the active dimer of E6AP.
External linksNat Commun / PubMed:38670961 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 5.1 Å
Structure data

36599

8jrn

EMDB-36599, PDB-8jrn:
Structure of E6AP-E6 complex in Att1 state
Method: EM (single particle) / Resolution: 2.6 Å

36600

8jro

EMDB-36600, PDB-8jro:
Structure of E6AP-E6 complex in Att2 state
Method: EM (single particle) / Resolution: 3.01 Å

36601

8jrp

EMDB-36601, PDB-8jrp:
Structure of E6AP-E6 complex in Att3 state
Method: EM (single particle) / Resolution: 3.58 Å

36602

8jrq

EMDB-36602, PDB-8jrq:
Structure of E6AP-E6 complex in Det1 state
Method: EM (single particle) / Resolution: 4.15 Å

36603

8jrr

EMDB-36603, PDB-8jrr:
Structure of E6AP-E6 complex in Det2 state
Method: EM (single particle) / Resolution: 4.35 Å

EMDB-36604: Structure of human full-length E6AP
Method: EM (single particle) / Resolution: 5.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • human papillomavirus 16
KeywordsLIGASE/ONCOPROTEIN / Complex / Viral protein / Tumor / LIGASE-ONCOPROTEIN 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