[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 basis of dynamic P5CS filaments.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateMar 14, 2022
AuthorsJiale Zhong / Chen-Jun Guo / Xian Zhou / Chia-Chun Chang / Boqi Yin / Tianyi Zhang / Huan-Huan Hu / Guang-Ming Lu / Ji-Long Liu /
PubMed AbstractThe bifunctional enzyme Δ-pyrroline-5-carboxylate synthase (P5CS) is vital to the synthesis of proline and ornithine, playing an essential role in human health and agriculture. Pathogenic mutations ...The bifunctional enzyme Δ-pyrroline-5-carboxylate synthase (P5CS) is vital to the synthesis of proline and ornithine, playing an essential role in human health and agriculture. Pathogenic mutations in the P5CS gene (ALDH18A1) lead to neurocutaneous syndrome and skin relaxation connective tissue disease in humans, and P5CS deficiency seriously damages the ability to resist adversity in plants. We have recently found that P5CS forms cytoophidia in vivo and filaments in vitro. However, it is difficult to appreciate the function of P5CS filamentation without precise structures. Using cryo-electron microscopy, here we solve the structures of full-length P5CS in three states at resolution from 3.1 to 4.3 Å. We observe distinct ligand-binding states and conformational changes for the GK and GPR domains, respectively. Divergent helical filaments are assembled by P5CS tetramers and stabilized by multiple interfaces. Point mutations disturbing those interfaces prevent P5CS filamentation and greatly reduce the enzymatic activity. Our findings reveal that filamentation is crucial for the coordination between the GK and GPR domains, providing a structural basis for the catalytic function of P5CS filaments.
External linksElife / PubMed:35286254 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.3 Å
Structure data

EMDB-31466, PDB-7f5t:
Drosophila P5CS filament with glutamate
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-31467, PDB-7f5u:
Drosophila P5CS filament with glutamate and ATPgammaS
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-31468, PDB-7f5v:
Drosophila P5CS filament with glutamate, ATP, and NADPH
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-31469, PDB-7f5x:
GK domain of Drosophila P5CS filament with glutamate
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-32875, PDB-7wx3:
GK domain of Drosophila P5CS filament with glutamate, ATP, and NADPH
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-32876, PDB-7wx4:
GK domain of Drosophila P5CS filament with glutamate and ATPgammaS
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-32877, PDB-7wxf:
GPR domain of Drosophila P5CS filament with glutamate
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-32878, PDB-7wxg:
GPR domain closed form of Drosophila P5CS filament with glutamate, ATP, and NADPH
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-32879, PDB-7wxh:
GPR domain open form of Drosophila P5CS filament with glutamate, ATP, and NADPH
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-32880, PDB-7wxi:
GPR domain of Drosophila P5CS filament with glutamate and ATPgammaS
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID / Glutamic acid

ChemComp-GGL:
GAMMA-L-GLUTAMIC ACID / Glutamic acid

ChemComp-RGP:
GAMMA-GLUTAMYL PHOSPHATE

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

ChemComp-MG:
Unknown entry

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

Source
  • drosophila melanogaster (fruit fly)
KeywordsTRANSFERASE / glutamate-bound / filament / ALDH18A1 / Delta-1-pyrroline-5-carboxylate synthase / BIOSYNTHETIC PROTEIN

+
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