[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

TitleSelf-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.
Journal, issue, pagesSci Adv, Vol. 8, Issue 42, Page eadd3914, Year 2022
Publish dateOct 21, 2022
AuthorsRichard M Hooy / Yuichiro Iwamoto / Dan A Tudorica / Xuefeng Ren / James H Hurley /
PubMed AbstractThe adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to ...The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1-positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection.
External linksSci Adv / PubMed:36269825 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution9.2 - 20.0 Å
Structure data

EMDB-26853, PDB-7ux3:
Asymmetric unit of AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated narrow membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.6 Å

EMDB-27181, PDB-8d4c:
beta-Arf1 mediated dimeric assembly of AP-1, Arf1, Nef complex within lattice on MHC-I lipopeptide incorporated narrow membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.3 Å

EMDB-27182, PDB-8d4d:
gamma-Arf1 mediated dimeric assembly of AP-1, Arf1, Nef complex within lattice on MHC-I lipopeptide incorporated narrow membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.6 Å

EMDB-27183, PDB-8d4e:
Asymmetric unit of AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated wide(r) membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.2 Å

EMDB-27184, PDB-8d4f:
beta-Arf1 mediated dimeric assembly of AP-1, Arf1, Nef complex within lattice on MHC-I lipopeptide incorporated wide(r) membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.8 Å

EMDB-27185, PDB-8d4g:
gamma-Arf1 mediated dimeric assembly of AP-1, Arf1, Nef complex within lattice on MHC-I lipopeptide incorporated wide(r) membrane tubes
Method: EM (subtomogram averaging) / Resolution: 11.6 Å

EMDB-27186: Beta-Arf1 homodimeric interface within AP-1 lattice on narrow membrane tubes
PDB-8d9w: beta-Arf1 homodimeric interface within AP-1, Arf1, Nef, MHC-I lattice on narrow tubes
Method: EM (subtomogram averaging) / Resolution: 9.3 Å

EMDB-27187: Gamma-Arf1 homodimeric interface within AP-1 lattice on narrow membrane tubes
PDB-8d9v: gamma-Arf1 homodimeric interface within AP-1, Arf1, Nef lattice on narrow membrane tubes
Method: EM (subtomogram averaging) / Resolution: 9.4 Å

EMDB-27188: Subtomogram average of AP-1, Arf1 and Nef complexes on narrow membrane tubes centered on beta-Arf1 dimers
PDB-8d9u: AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated narrow membrane tubes, centered on beta-Arf1
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

EMDB-27189: Subtomogram average of AP-1, Arf1 and Nef complexes on narrow membrane tubes centered on gamma-Arf1 dimers
PDB-8d9t: AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated narrow membrane tubes, centered on gamma-Arf1
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

EMDB-27190: Subtomogram average of AP-1, Arf1 and Nef complexes on wide(r) membrane tubes centered on beta-Arf1 dimers
PDB-8d9s: AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated wide membrane tubes, centered on beta-Arf1
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

EMDB-27191: Subtomogram average of AP-1, Arf1 and Nef complexes on wide(r) membrane tubes centered on gamma-Arf1 dimers
PDB-8d9r: AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated wide membrane tubes, centered on gamma-Arf1
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN/PROTEIN TRANSPORT / nef / AP / HIV / trafficking / VIRAL PROTEIN / VIRAL PROTEIN-PROTEIN TRANSPORT complex / PROTEIN TRANSPORT / Protein Transport/Viral Protein / complex / coat / Protein Transport-Viral Protein 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