[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

TitleAsymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex.
Journal, issue, pagesCell, Vol. 180, Issue 1, Page 165-175.e16, Year 2020
Publish dateJan 9, 2020
AuthorsMichal Wieczorek / Linas Urnavicius / Shih-Chieh Ti / Kelly R Molloy / Brian T Chait / Tarun M Kapoor /
PubMed AbstractThe γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the ...The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human γ-TuRC at ∼3.8 Å resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the γ-TuRC "seam." We also identify an unanticipated structural bridge that includes an actin-like protein and spans the γ-TuRC lumen. Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the γ-TuRC subunits introduces large (>100,000 Å) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the γ-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments.
External linksCell / PubMed:31862189 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 6.6 Å
Structure data

21054

6v5v

EMDB-21054, PDB-6v5v:
Structure of gamma-tubulin in the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 3.8 Å

21060

6v69

EMDB-21060, PDB-6v69:
Structures of GCP4 and GCP5 in the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-21063:
Density map surrounding actin-like protein in reconstruction of the native gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 4.1 Å

21067

6v6b

EMDB-21067, PDB-6v6b:
Structures of GCP2 and GCP3 in the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 3.8 Å

21068

6v6c

EMDB-21068, PDB-6v6c:
Structure of GCP6 in the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-21069:
Desnity map of lumenal bridge in reconstruction of the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-21070:
Density map for overlap region in reconstruction of native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 6.6 Å

21073

6v6s

EMDB-21073, PDB-6v6s:
Structure of the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-21074:
Overall density map of the native human gamma-tubulin ring complex
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / Tubulin / gamma-tubulin / gamma-tubulin ring complex / gTuRC / g-TuRC / microtubule / microtubule nucleation / single particle cryo-EM structure / GCP / GCP4 / GCP5 / GCP2 / GCP3 / gamma-TuSC / gTuSC / GCP6

+
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