Molecular basis for interactions between an acyl carrier protein and a ketosynthase.
Nat Chem Biol
; 15(7): 669-671, 2019 07.
Article
in En
| MEDLINE
| ID: mdl-31209348
ABSTRACT
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 ß-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.
Full text:
1
Database:
MEDLINE
Main subject:
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
/
Acyl Carrier Protein
/
Escherichia coli Proteins
/
Fatty Acid Synthase, Type II
Language:
En
Journal:
Nat Chem Biol
Journal subject:
BIOLOGIA
/
QUIMICA
Year:
2019
Type:
Article
Affiliation country:
United States