The cryo-EM structure of the chloroplast ClpP complex.
Journal
Nature plants
ISSN: 2055-0278
Titre abrégé: Nat Plants
Pays: England
ID NLM: 101651677
Informations de publication
Date de publication:
11 2021
11 2021
Historique:
received:
03
11
2020
accepted:
12
10
2021
entrez:
16
11
2021
pubmed:
17
11
2021
medline:
27
1
2022
Statut:
ppublish
Résumé
Protein homoeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here, we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtii by cryo-electron microscopy. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1
Identifiants
pubmed: 34782772
doi: 10.1038/s41477-021-01020-x
pii: 10.1038/s41477-021-01020-x
doi:
Substances chimiques
Chaperonins
EC 3.6.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1505-1515Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Nature Limited.
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