Steric occlusion regulates proximal interactions of acyl carrier protein domain in fungal fatty acid synthase.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
29 05 2020
29 05 2020
Historique:
received:
15
01
2020
accepted:
06
05
2020
entrez:
31
5
2020
pubmed:
31
5
2020
medline:
16
6
2021
Statut:
epublish
Résumé
The acyl carrier protein (ACP) domain shuttles substrates and reaction intermediates in type I fungal fatty acid synthases via transient protein-protein interactions. Here, using electron cryo-microscopy (cryoEM), we report the structure of a fungal FAS stalled at the dehydration reaction, which precedes the final enoyl reduction in the fatty acid biosynthesis cycle. This conformation revealed multiple contact sites between ACP and the dehydratase (DH) and enoyl reductase (ER) domains that occluded the ACP binding to the adjacent ER domain. Our data suggests a minimal path from the DH to the ER reaction site that requires minute changes in the coordinates of the structured N- and C- termini of the ACP domain.
Identifiants
pubmed: 32471977
doi: 10.1038/s42003-020-0997-y
pii: 10.1038/s42003-020-0997-y
pmc: PMC7260205
doi:
Substances chimiques
Acyl Carrier Protein
0
Fatty Acid Synthases
EC 2.3.1.85
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
274Subventions
Organisme : CIHR
ID : 419240
Pays : Canada
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