Molecular basis for interactions between an acyl carrier protein and a ketosynthase.
Journal
Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976
Informations de publication
Date de publication:
07 2019
07 2019
Historique:
received:
23
02
2018
accepted:
01
05
2019
pubmed:
19
6
2019
medline:
18
7
2019
entrez:
19
6
2019
Statut:
ppublish
Résumé
Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli.
Identifiants
pubmed: 31209348
doi: 10.1038/s41589-019-0301-y
pii: 10.1038/s41589-019-0301-y
pmc: PMC7323458
mid: NIHMS1596415
doi:
Substances chimiques
Acyl Carrier Protein
0
Escherichia coli Proteins
0
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
EC 2.3.1.41
FabB protein, E coli
EC 2.3.1.41
Fatty Acid Synthase, Type II
EC 6.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
669-671Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM108561
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM079383
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM100305
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM095970
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM093040
Pays : United States
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